Gene regulation in eukaryotes in a nutshell covering all the important stages of gene regulation in eukaryotes at transcriptional level, translation level and post-translational level.
This document discusses eukaryotic chromosome organization. It notes that eukaryotic cells contain many chromosomes in the nucleus, with each species having a characteristic number. Chromosomes are made up of DNA and proteins like histones. DNA is wrapped around histones to form structures called nucleosomes, which are further compacted through multiple levels of coiling and folding involving other proteins. This allows the long DNA molecules to fit within cell nuclei.
This document discusses the structures and functions of heterochromatin and euchromatin. Heterochromatin is tightly packed and transcriptionally inactive, found near centromeres and telomeres. Euchromatin is loosely packed and contains most actively transcribed genes. The basic unit of DNA packing is the nucleosome, which involves DNA wound around histone proteins. Heterochromatin and euchromatin differ in their genetic activity, location within chromosomes, and condensation levels during interphase.
The document discusses protein synthesis and post-translational modification. It describes how translation involves mRNA, ribosomes, tRNA, and release factors to synthesize proteins. The process involves initiation, elongation, and termination. After synthesis, the peptide undergoes folding, modification like phosphorylation, and can be transported to organelles. Post-translational modifications are important for diversity and regulating protein function, and involve processes like methylation, ubiquitination, and glycosylation. Diseases like atherosclerosis and fibrosis are related to disorders of collagen deposition and modification.
Transcription in eukaryotes: A brief view
Transcription is the process by which single stranded RNA is synthesized by double stranded DNA. Transcription in eukaryotes and prokaryotes has many similarities while at the same time both showing their individual characteristics due to the differences in organization. RNA Polymerase (RNAP or RNA Pol) is different in prokaryotes and eukaryotes. Coupled transcription is seen in prokaryotes but not in Eukaryotes. In eukaryotes the pre-RNA should be spliced first to be translated.
In Eukaryotic transcription, synthesis of RNA occurs in the 3’→5’ direction. The 3’ end is more reactive due to the hydroxide group. 5’ end containing phosphate groups meanwhile, is not very reactive when it comes to adding new nucleotides. In Eukaryotes, the whole genome is not transcribed at once. Only a part of the genome is transcribed which also acts as the first, principle stage of genetic regulation.
Eukaryotes have five nuclear polymerases:
• RNA Polymerase I: This produces rRNA (23S, 5.8S, and 18S) which are the major components in a ribosome. This also produces pre-rRNA in yeasts.
• RNA Polymerase II: Helps in the production of mRNA (messenger RNA), snRNA (small, nuclear RNA), miRNA. This is the most studied type and requires several transcription factors for its binding
• RNA Polymerase III: This synthesizes tRNA (transfer RNA), 5S rRNA and other small RNAs required in the cytosol and nucleus.
• RNA Polymerase IV: Synthesizes siRNA (small interfering RNA) in plants.
• RNA Polymerase V: This is the least studied polymerase and synthesizes siRNA-directed heterochromatin in plants.
Eukaryotic transcription can be broadly divided into 4 stages:
• Pre-Initiation
• Initiation
• Elongation
• Termination
Transcription is an elaborate process which cells use to copy the genetic information stored in DNA into RNA. This pre-RNA is modified into mRNA before being transcribed to proteins. Transcription is the first step to utilizing the genetic information in a cell. Both Eukaryotes and Prokaryotes employ this process with the basic phases remaining the same. However eukaryotic transcription is more complex indicating the changes transcription has undergone towards perfection during evolution.
The tryptophan operon regulates the biosynthesis of tryptophan in E. coli through transcriptional attenuation and repression. It contains five genes encoding the enzymes needed to synthesize tryptophan. When tryptophan levels are high, the tryptophan repressor binds to the operator site, preventing transcription. Additionally, a regulatory region can form a terminator stem-loop structure to halt transcription if tryptophan tRNA levels are high during translation of the leader mRNA sequence. However, if tryptophan levels are low, the terminator structure does not form and transcription of the operon proceeds.
Molecular biology is the study of biology at a molecular level.
In broad sense, the study of gene structure and functions at the molecular level to understand the molecular basis of hereditary, genetic variation, and the expression patterns of genes.The field overlaps with other areas of biology and chemistry, particularly genetics and biochemistry.
This document discusses the structure and function of chromatin. It begins with a history of chromatin discovery from 1878-1974. Chromatin is composed of DNA, histones, and non-histone proteins. There are two types of chromatin - heterochromatin, which is condensed and inactive, and euchromatin, which is less condensed and contains actively transcribed genes. Chromatin replicates during interphase and condenses further during mitosis. DNA is packaged into nucleosomes, which involve 147 base pairs of DNA wrapped around an octamer of histone proteins, and these compact to form chromatin fibers and chromosomes. The functions of chromatin include efficient DNA packaging, facilitating cell division, preventing chromosome breakage, and regulating gene expression.
Gene regulation in eukaryotes in a nutshell covering all the important stages of gene regulation in eukaryotes at transcriptional level, translation level and post-translational level.
This document discusses eukaryotic chromosome organization. It notes that eukaryotic cells contain many chromosomes in the nucleus, with each species having a characteristic number. Chromosomes are made up of DNA and proteins like histones. DNA is wrapped around histones to form structures called nucleosomes, which are further compacted through multiple levels of coiling and folding involving other proteins. This allows the long DNA molecules to fit within cell nuclei.
This document discusses the structures and functions of heterochromatin and euchromatin. Heterochromatin is tightly packed and transcriptionally inactive, found near centromeres and telomeres. Euchromatin is loosely packed and contains most actively transcribed genes. The basic unit of DNA packing is the nucleosome, which involves DNA wound around histone proteins. Heterochromatin and euchromatin differ in their genetic activity, location within chromosomes, and condensation levels during interphase.
The document discusses protein synthesis and post-translational modification. It describes how translation involves mRNA, ribosomes, tRNA, and release factors to synthesize proteins. The process involves initiation, elongation, and termination. After synthesis, the peptide undergoes folding, modification like phosphorylation, and can be transported to organelles. Post-translational modifications are important for diversity and regulating protein function, and involve processes like methylation, ubiquitination, and glycosylation. Diseases like atherosclerosis and fibrosis are related to disorders of collagen deposition and modification.
Transcription in eukaryotes: A brief view
Transcription is the process by which single stranded RNA is synthesized by double stranded DNA. Transcription in eukaryotes and prokaryotes has many similarities while at the same time both showing their individual characteristics due to the differences in organization. RNA Polymerase (RNAP or RNA Pol) is different in prokaryotes and eukaryotes. Coupled transcription is seen in prokaryotes but not in Eukaryotes. In eukaryotes the pre-RNA should be spliced first to be translated.
In Eukaryotic transcription, synthesis of RNA occurs in the 3’→5’ direction. The 3’ end is more reactive due to the hydroxide group. 5’ end containing phosphate groups meanwhile, is not very reactive when it comes to adding new nucleotides. In Eukaryotes, the whole genome is not transcribed at once. Only a part of the genome is transcribed which also acts as the first, principle stage of genetic regulation.
Eukaryotes have five nuclear polymerases:
• RNA Polymerase I: This produces rRNA (23S, 5.8S, and 18S) which are the major components in a ribosome. This also produces pre-rRNA in yeasts.
• RNA Polymerase II: Helps in the production of mRNA (messenger RNA), snRNA (small, nuclear RNA), miRNA. This is the most studied type and requires several transcription factors for its binding
• RNA Polymerase III: This synthesizes tRNA (transfer RNA), 5S rRNA and other small RNAs required in the cytosol and nucleus.
• RNA Polymerase IV: Synthesizes siRNA (small interfering RNA) in plants.
• RNA Polymerase V: This is the least studied polymerase and synthesizes siRNA-directed heterochromatin in plants.
Eukaryotic transcription can be broadly divided into 4 stages:
• Pre-Initiation
• Initiation
• Elongation
• Termination
Transcription is an elaborate process which cells use to copy the genetic information stored in DNA into RNA. This pre-RNA is modified into mRNA before being transcribed to proteins. Transcription is the first step to utilizing the genetic information in a cell. Both Eukaryotes and Prokaryotes employ this process with the basic phases remaining the same. However eukaryotic transcription is more complex indicating the changes transcription has undergone towards perfection during evolution.
The tryptophan operon regulates the biosynthesis of tryptophan in E. coli through transcriptional attenuation and repression. It contains five genes encoding the enzymes needed to synthesize tryptophan. When tryptophan levels are high, the tryptophan repressor binds to the operator site, preventing transcription. Additionally, a regulatory region can form a terminator stem-loop structure to halt transcription if tryptophan tRNA levels are high during translation of the leader mRNA sequence. However, if tryptophan levels are low, the terminator structure does not form and transcription of the operon proceeds.
Molecular biology is the study of biology at a molecular level.
In broad sense, the study of gene structure and functions at the molecular level to understand the molecular basis of hereditary, genetic variation, and the expression patterns of genes.The field overlaps with other areas of biology and chemistry, particularly genetics and biochemistry.
This document discusses the structure and function of chromatin. It begins with a history of chromatin discovery from 1878-1974. Chromatin is composed of DNA, histones, and non-histone proteins. There are two types of chromatin - heterochromatin, which is condensed and inactive, and euchromatin, which is less condensed and contains actively transcribed genes. Chromatin replicates during interphase and condenses further during mitosis. DNA is packaged into nucleosomes, which involve 147 base pairs of DNA wrapped around an octamer of histone proteins, and these compact to form chromatin fibers and chromosomes. The functions of chromatin include efficient DNA packaging, facilitating cell division, preventing chromosome breakage, and regulating gene expression.
This document provides an overview of the central dogma and genetic code. It discusses how DNA is transcribed into mRNA which is then translated into proteins. The genetic code uses triplets of nucleotides called codons to specify the 20 amino acids. There are 64 possible codons but only 61 encode amino acids, while 3 serve as stop signals. The code is degenerate, universal and read in a consistent direction. The wobble hypothesis explains how one tRNA can recognize multiple codons. Mutations can alter codons and result in silent, missense or nonsense changes impacting protein synthesis.
The trp operon contains a cluster of genes involved in tryptophan biosynthesis that are under the control of a single promoter. It was the first repressible operon discovered in E. coli in 1953. The trp operon contains structural genes that encode enzymes for tryptophan synthesis, as well as a promoter, operator, and regulatory genes. Tryptophan acts as an effector molecule that binds to the repressor protein, increasing its affinity for the operator sequence and repressing transcription when tryptophan is present. The trp operon is also regulated by transcriptional attenuation, where tryptophan levels affect the formation of termination or anti-termination hairpin loops in the mRNA.
Genetic code, Deciphering of genetic code, properties of genetic code, Initiation & termination of codons, Gene Mutation, non sense codon, release factors, Transition , Trans versions
In eukaryotic cells, DNA is packaged through interactions with histone proteins to form nucleosomes, which are beads of DNA wound around histone octamers. Nucleosomes further condense into chromatin, and additional non-histone proteins compact chromatin into higher-order structures. In prokaryotes, DNA is loosely organized into loops associated with proteins in the nucleoid region, which lacks a membrane-bound nucleus. Eukaryotic chromatin also exists in two forms - loosely coiled euchromatin containing active genes, and tightly packed heterochromatin containing inactive regions.
The document discusses transcription in prokaryotes and eukaryotes. In prokaryotes, RNA polymerase binds to promoter sequences and transcribes DNA into RNA through initiation, elongation, and termination. Transcription requires RNA polymerase and proceeds similarly in eukaryotes but involves multiple RNA polymerases and occurs in the nucleus. Eukaryotic transcription is more complex, utilizing regulatory sequences, transcription factors, and RNA processing to modify pre-mRNA into mature mRNA through splicing, capping, polyadenylation, and other modifications. Mutations can affect splicing and cause genetic disorders like beta-thalassemia.
Genetic code is the term we use for the way that the four bases of DNA--the A, C, G, and Ts--are strung together in a way that the cellular machinery, the ribosome, can read them and turn them into a protein. In the genetic code, each three nucleotides in a row count as a triplet and code for a single amino acid.
This document discusses the central dogma of biology and the process of transcription. It describes the three main steps of transcription - initiation, elongation, and termination. Initiation involves the RNA polymerase binding to the promoter sequence on DNA and separating the DNA strands to form an open complex. Elongation is the addition of nucleotides to synthesize RNA. Termination can occur via either Rho-independent or Rho-dependent mechanisms, with the former utilizing a terminator sequence and hairpin structure in the RNA and the latter involving the Rho protein.
Protein targeting involves transporting proteins to their proper destinations after synthesis so they can perform their functions. There are two main pathways: co-translational targeting transports proteins during translation to the ER, Golgi and secretory pathway, while post-translational targeting transports proteins after translation to the nucleus, mitochondria and peroxisomes. Targeting sequences on the protein interact with receptors to mediate transport through membrane channels using energy from GTP or ATP hydrolysis. Defects in protein targeting can cause diseases like Zellweger syndrome, primary hyperoxaluria and cystic fibrosis.
watson and crick model of DNA(molecular biology) IndrajaDoradla
The document summarizes the Watson and Crick model of DNA, which proposed in 1953 that DNA consists of two helical strands coiled around a common axis to form a double helix. Each strand contains alternating sugar and phosphate groups, with nitrogenous base pairs connecting the strands via hydrogen bonds. Adenine always pairs with thymine and guanine pairs with cytosine. The structure explained DNA's ability to replicate itself accurately during cell division. Rosalind Franklin's X-ray diffraction images provided key evidence for the double helix structure, though she did not receive full credit at the time due to sexism in the field.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
The document summarizes transcription in eukaryotes. It discusses that eukaryotes have three RNA polymerases - Pol I, Pol II, and Pol III. Pol II is responsible for transcribing protein-encoding genes and requires general transcription factors for initiation. Transcription involves initiation, elongation, and termination phases. The RNA polymerase forms a pre-initiation complex at the promoter and then adds nucleotides during elongation. Termination occurs after RNA processing and polyadenylation.
Eukaryotic genomes are organized into chromatin and packaged at successive levels. DNA is wrapped around histone proteins to form nucleosomes, which are further packaged into higher-order structures like the 30nm fiber and loop domains. These domains are attached to scaffolding proteins, forming interphase chromosome territories and mitotic chromosomes. Precise packaging allows for gene expression control and proper chromosome segregation during cell division. Telomeres and histone modifications also influence chromatin structure and gene regulation.
Telomeres are repetitive DNA sequences at the ends of chromosomes that protect chromosomal integrity. Each cell division causes telomeres to shorten as DNA replication cannot fully copy chromosome ends. When telomeres become too short, cells stop dividing or die. Telomerase is an enzyme that adds telomeric DNA to chromosome ends and counteracts shortening. While most somatic cells lack telomerase, its presence allows cancer cells and germ cells to avoid replicative aging. Maintaining telomere length through telomerase overexpression is a hallmark of cancer cells and targeting this process may lead to new anticancer therapies.
The genetic code is the system by which nucleotide sequences in mRNA determine the amino acid sequences in proteins. The genetic code uses triplets of nucleotides called codons to specify which amino acid will be incorporated into the growing polypeptide chain. There are 64 possible codons but only 20 standard amino acids, so most amino acids have multiple codons. Three codons act as stop signals to end protein synthesis. The genetic code is nearly universal across all life due to its high degree of specificity and redundancy.
The document summarizes eukaryotic DNA replication. It discusses that DNA replication in eukaryotes is more complex than prokaryotes due to larger genome size and chromatin packaging. The key stages of eukaryotic replication are similar to prokaryotes, including origin of replication, formation of replication forks, semiconservative replication and synthesis of leading and lagging strands. However, eukaryotic replication involves additional proteins and is slower due to chromatin remodeling required to access DNA.
"Introns: Structure and Functions" during November, 2011 (Friday Seminar activity, Department of Biotechnology, University of Agricultural Sciences, Dharwad, Karnataka) by Yogesh S Bhagat (Ph D Scholar)
A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA replication and usually work in groups to create two identical DNA duplexes from a single original DNA duplex. During this process, DNA polymerase "reads" the existing DNA strands to create two new strands that match the existing ones.[1][2][3][4][5][6] These enzymes catalyze the chemical reaction
deoxynucleoside triphosphate + DNAn ⇌ pyrophosphate + DNAn+1.
DNA polymerase adds nucleotides to the three prime (3')-end of a DNA strand, one nucleotide at a time. Every time a cell divides, DNA polymerases are required to duplicate the cell's DNA, so that a copy of the original DNA molecule can be passed to each daughter cell. In this way, genetic information is passed down from generation to generation.
Before replication can take place, an enzyme called helicase unwinds the DNA molecule from its tightly woven form, in the process breaking the hydrogen bonds between the nucleotide bases. This opens up or "unzips" the double-stranded DNA to give two single strands of DNA that can be used as templates for replication in the above reaction.
DNA replication in prokaryotes begins with the unwinding of DNA at the origin of replication by enzymes like DnaA and DnaB helicase. This produces two replication forks that move in opposite directions. The leading strand is replicated continuously while the lagging strand is replicated discontinuously in short segments called Okazaki fragments. DNA polymerase III is the main enzyme that synthesizes new DNA. Replication terminates at the terminus region when the DnaB helicase is stopped by protein Tus bound to Ter sequences.
The document discusses the genetic code, which is the set of rules by which DNA and mRNA sequences are translated into amino acid sequences in proteins. Some key points are:
- The genetic code is made up of 3 nucleotide sequences called codons that each encode for a specific amino acid.
- The code is degenerate, meaning most amino acids are encoded by more than one codon.
- Experiments in the 1960s were the first to demonstrate that the genetic code consists of codons that are three nucleotides long and elucidated the nature of the codon-amino acid relationship.
The sequence of nucleotides in deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) that determines the amino acid sequence of proteins. Though the linear sequence of nucleotides in DNA contains the information for protein sequences, proteins are not made directly from DNA. Instead, a messenger RNA (mRNA) molecule is synthesized from the DNA and directs the formation of the protein. RNA is composed of four nucleotides: adenine (A), guanine (G), cytosine (C), and uracil."(U)."
This document provides an overview of the central dogma and genetic code. It discusses how DNA is transcribed into mRNA which is then translated into proteins. The genetic code uses triplets of nucleotides called codons to specify the 20 amino acids. There are 64 possible codons but only 61 encode amino acids, while 3 serve as stop signals. The code is degenerate, universal and read in a consistent direction. The wobble hypothesis explains how one tRNA can recognize multiple codons. Mutations can alter codons and result in silent, missense or nonsense changes impacting protein synthesis.
The trp operon contains a cluster of genes involved in tryptophan biosynthesis that are under the control of a single promoter. It was the first repressible operon discovered in E. coli in 1953. The trp operon contains structural genes that encode enzymes for tryptophan synthesis, as well as a promoter, operator, and regulatory genes. Tryptophan acts as an effector molecule that binds to the repressor protein, increasing its affinity for the operator sequence and repressing transcription when tryptophan is present. The trp operon is also regulated by transcriptional attenuation, where tryptophan levels affect the formation of termination or anti-termination hairpin loops in the mRNA.
Genetic code, Deciphering of genetic code, properties of genetic code, Initiation & termination of codons, Gene Mutation, non sense codon, release factors, Transition , Trans versions
In eukaryotic cells, DNA is packaged through interactions with histone proteins to form nucleosomes, which are beads of DNA wound around histone octamers. Nucleosomes further condense into chromatin, and additional non-histone proteins compact chromatin into higher-order structures. In prokaryotes, DNA is loosely organized into loops associated with proteins in the nucleoid region, which lacks a membrane-bound nucleus. Eukaryotic chromatin also exists in two forms - loosely coiled euchromatin containing active genes, and tightly packed heterochromatin containing inactive regions.
The document discusses transcription in prokaryotes and eukaryotes. In prokaryotes, RNA polymerase binds to promoter sequences and transcribes DNA into RNA through initiation, elongation, and termination. Transcription requires RNA polymerase and proceeds similarly in eukaryotes but involves multiple RNA polymerases and occurs in the nucleus. Eukaryotic transcription is more complex, utilizing regulatory sequences, transcription factors, and RNA processing to modify pre-mRNA into mature mRNA through splicing, capping, polyadenylation, and other modifications. Mutations can affect splicing and cause genetic disorders like beta-thalassemia.
Genetic code is the term we use for the way that the four bases of DNA--the A, C, G, and Ts--are strung together in a way that the cellular machinery, the ribosome, can read them and turn them into a protein. In the genetic code, each three nucleotides in a row count as a triplet and code for a single amino acid.
This document discusses the central dogma of biology and the process of transcription. It describes the three main steps of transcription - initiation, elongation, and termination. Initiation involves the RNA polymerase binding to the promoter sequence on DNA and separating the DNA strands to form an open complex. Elongation is the addition of nucleotides to synthesize RNA. Termination can occur via either Rho-independent or Rho-dependent mechanisms, with the former utilizing a terminator sequence and hairpin structure in the RNA and the latter involving the Rho protein.
Protein targeting involves transporting proteins to their proper destinations after synthesis so they can perform their functions. There are two main pathways: co-translational targeting transports proteins during translation to the ER, Golgi and secretory pathway, while post-translational targeting transports proteins after translation to the nucleus, mitochondria and peroxisomes. Targeting sequences on the protein interact with receptors to mediate transport through membrane channels using energy from GTP or ATP hydrolysis. Defects in protein targeting can cause diseases like Zellweger syndrome, primary hyperoxaluria and cystic fibrosis.
watson and crick model of DNA(molecular biology) IndrajaDoradla
The document summarizes the Watson and Crick model of DNA, which proposed in 1953 that DNA consists of two helical strands coiled around a common axis to form a double helix. Each strand contains alternating sugar and phosphate groups, with nitrogenous base pairs connecting the strands via hydrogen bonds. Adenine always pairs with thymine and guanine pairs with cytosine. The structure explained DNA's ability to replicate itself accurately during cell division. Rosalind Franklin's X-ray diffraction images provided key evidence for the double helix structure, though she did not receive full credit at the time due to sexism in the field.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
The document summarizes transcription in eukaryotes. It discusses that eukaryotes have three RNA polymerases - Pol I, Pol II, and Pol III. Pol II is responsible for transcribing protein-encoding genes and requires general transcription factors for initiation. Transcription involves initiation, elongation, and termination phases. The RNA polymerase forms a pre-initiation complex at the promoter and then adds nucleotides during elongation. Termination occurs after RNA processing and polyadenylation.
Eukaryotic genomes are organized into chromatin and packaged at successive levels. DNA is wrapped around histone proteins to form nucleosomes, which are further packaged into higher-order structures like the 30nm fiber and loop domains. These domains are attached to scaffolding proteins, forming interphase chromosome territories and mitotic chromosomes. Precise packaging allows for gene expression control and proper chromosome segregation during cell division. Telomeres and histone modifications also influence chromatin structure and gene regulation.
Telomeres are repetitive DNA sequences at the ends of chromosomes that protect chromosomal integrity. Each cell division causes telomeres to shorten as DNA replication cannot fully copy chromosome ends. When telomeres become too short, cells stop dividing or die. Telomerase is an enzyme that adds telomeric DNA to chromosome ends and counteracts shortening. While most somatic cells lack telomerase, its presence allows cancer cells and germ cells to avoid replicative aging. Maintaining telomere length through telomerase overexpression is a hallmark of cancer cells and targeting this process may lead to new anticancer therapies.
The genetic code is the system by which nucleotide sequences in mRNA determine the amino acid sequences in proteins. The genetic code uses triplets of nucleotides called codons to specify which amino acid will be incorporated into the growing polypeptide chain. There are 64 possible codons but only 20 standard amino acids, so most amino acids have multiple codons. Three codons act as stop signals to end protein synthesis. The genetic code is nearly universal across all life due to its high degree of specificity and redundancy.
The document summarizes eukaryotic DNA replication. It discusses that DNA replication in eukaryotes is more complex than prokaryotes due to larger genome size and chromatin packaging. The key stages of eukaryotic replication are similar to prokaryotes, including origin of replication, formation of replication forks, semiconservative replication and synthesis of leading and lagging strands. However, eukaryotic replication involves additional proteins and is slower due to chromatin remodeling required to access DNA.
"Introns: Structure and Functions" during November, 2011 (Friday Seminar activity, Department of Biotechnology, University of Agricultural Sciences, Dharwad, Karnataka) by Yogesh S Bhagat (Ph D Scholar)
A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA replication and usually work in groups to create two identical DNA duplexes from a single original DNA duplex. During this process, DNA polymerase "reads" the existing DNA strands to create two new strands that match the existing ones.[1][2][3][4][5][6] These enzymes catalyze the chemical reaction
deoxynucleoside triphosphate + DNAn ⇌ pyrophosphate + DNAn+1.
DNA polymerase adds nucleotides to the three prime (3')-end of a DNA strand, one nucleotide at a time. Every time a cell divides, DNA polymerases are required to duplicate the cell's DNA, so that a copy of the original DNA molecule can be passed to each daughter cell. In this way, genetic information is passed down from generation to generation.
Before replication can take place, an enzyme called helicase unwinds the DNA molecule from its tightly woven form, in the process breaking the hydrogen bonds between the nucleotide bases. This opens up or "unzips" the double-stranded DNA to give two single strands of DNA that can be used as templates for replication in the above reaction.
DNA replication in prokaryotes begins with the unwinding of DNA at the origin of replication by enzymes like DnaA and DnaB helicase. This produces two replication forks that move in opposite directions. The leading strand is replicated continuously while the lagging strand is replicated discontinuously in short segments called Okazaki fragments. DNA polymerase III is the main enzyme that synthesizes new DNA. Replication terminates at the terminus region when the DnaB helicase is stopped by protein Tus bound to Ter sequences.
The document discusses the genetic code, which is the set of rules by which DNA and mRNA sequences are translated into amino acid sequences in proteins. Some key points are:
- The genetic code is made up of 3 nucleotide sequences called codons that each encode for a specific amino acid.
- The code is degenerate, meaning most amino acids are encoded by more than one codon.
- Experiments in the 1960s were the first to demonstrate that the genetic code consists of codons that are three nucleotides long and elucidated the nature of the codon-amino acid relationship.
The sequence of nucleotides in deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) that determines the amino acid sequence of proteins. Though the linear sequence of nucleotides in DNA contains the information for protein sequences, proteins are not made directly from DNA. Instead, a messenger RNA (mRNA) molecule is synthesized from the DNA and directs the formation of the protein. RNA is composed of four nucleotides: adenine (A), guanine (G), cytosine (C), and uracil."(U)."
Genetic code is a dictionary that corresponds with sequence of nucleotides and sequence of amino acids.
Genetic code is a set of rules by which information encoded in genetic material(DNA or RNA sequences) is translated into proteins by living cells.
Term given By ″ Goerge Gamow ʺ
This document discusses the structure of genes in prokaryotes and eukaryotes. It defines a gene as a sequence of DNA that codes for a specific protein. Prokaryotic genes are continuous with three regions - a promoter, coding sequence, and terminator. Eukaryotic genes can be complex with introns and exons, promoters, terminators, and other regulatory elements. Key differences between prokaryotic and eukaryotic genes include the presence of introns and alternative splicing in eukaryotes. The document also outlines several characteristics of genes like their organization, transmission, mutation, and self-duplication.
This document discusses the structure of genes in prokaryotes and eukaryotes. It defines a gene as a sequence of DNA that codes for a specific protein. Prokaryotic genes are continuous with three regions - a promoter, coding sequence, and terminator. Eukaryotic genes can be complex with introns and exons, promoters, and regulatory elements. Key differences are that prokaryotic genes lack introns while eukaryotic genes undergo splicing to remove introns. The document also outlines several characteristics of genes like their transmission from parents to offspring and ability to mutate.
The genetic code is the set of rules by which genetic material like DNA and mRNA are translated into amino acid sequences that make up proteins. The genetic code specifies which amino acid will be added next during protein synthesis using sequences of three nucleotides called codons. While some codons specify the same amino acid, meaning the code is degenerate, this allows more codons to exist without increasing the number of amino acids used. Efforts to understand the genetic code increased after the discovery of DNA's structure, with scientists like Gamow theorizing it must use three nucleotides to code for the 20 standard amino acids.
The genetic code is the set of rules by which information encoded in genes flows from DNA to RNA and is translated into proteins. It is a universal dictionary that specifies which triplet of nucleotides (codon) corresponds to each amino acid. The genetic code is unambiguous, degenerate, non-overlapping, and universal in all living organisms. It specifies 64 codons, 61 of which encode the 20 standard amino acids. Three codons are stop codons, which terminate protein synthesis. Mutations in the genetic code can result in silent, missense, nonsense, or frameshift changes to the resulting protein.
STRUCTURE OF GENE and genetic code in animals pptIrfanBhat44
Structure of gene and genetic code
It permits essentially the same complement of enzymes and other proteins to be specified by microorganisms varying widely in their DNA base composition.
Degeneracy also provides a mechanism of minimising mutational lethality.
The genetic code is the sequence of nitrogen bases in mRNA that contains the information for protein synthesis. A codon is three nitrogen bases that code for a single amino acid. Nirenberg and Mathaei experimentally proved that codons determine amino acids. The genetic code is universal, uses non-overlapping triplets to specify amino acids in a linear, commaless fashion, and employs initiation and termination codons.
This presentation discusses the genetic code and how it translates DNA and RNA sequences into proteins. The genetic code is universal across all living organisms and consists of 64 codons composed of 3 nucleotides that correspond to 20 amino acids. Codons are classified as sense codons, which code for amino acids, or signal codons like initiation and termination codons. Anticodons on tRNAs pair with mRNA codons to recognize and translate the codons. The genetic code is non-overlapping, degenerate, and Francis Crick's wobble hypothesis explains the pattern of degeneracy by proposing the third position in the anticodon is not as specific.
1) The document discusses the genetic code, which determines how DNA and mRNA sequences are translated into proteins.
2) Marshall Nirenberg and others were the first to elucidate the nature of codons in 1961 and determine that codons consist of three DNA bases.
3) The genetic code is universal, uses triplets of nucleotides, has no commas, does not overlap, is not ambiguous, but is degenerate meaning several codons can code for the same amino acid.
The genetic code is a nonoverlapping code, with each amino acid plus polypeptide initiation and termination specified by RNA codons composed of three nucleotides.
DNA contains the genetic code that directs protein synthesis. The genetic code is stored in the sequence of nitrogen bases (A, T, C, G) in DNA. It was discovered that the genetic code uses triplets of these bases, called codons, to specify the 20 different amino acids used to build proteins. Experiments by Nirenberg and Khorana helped decipher the genetic code by artificially synthesizing RNA sequences and determining which amino acids they coded for. The genetic code was found to be nearly universal across all life, using 64 codons to specify amino acids or termination of protein synthesis.
Fredric Sanger determined the first protein sequence in 1953, which was insulin. There are two main methods for protein sequencing - N-terminal sequencing including the Sanger method and Edman degradation, and C-terminal sequencing using carboxypeptidases. Protein sequences can be predicted from DNA sequences after determining the gene sequence. Comparing protein sequences between organisms can provide information about evolutionary relationships and how organisms have diverged over time as mutations cause amino acid changes. Work has been done in Pakistan on sequencing various proteins.
The genetic code refers to the sequence of three nucleotides in RNA that determines the amino acid sequence of proteins. Evidence showed that changes in nucleotides led to changes in amino acids, leading to the proposal of a genetic code. The genetic code was deciphered by determining that codons are triplets of three bases that code for amino acids. Scientists like George Gamow, Har Gobind Khorana, and Marshall Nirenberg helped discover that there are 64 possible codons that code for 20 amino acids. The genetic code is nearly universal, with some exceptions, and has key features like being triplet-based, non-overlapping, and read sequentially from the 5' to 3' end of mRNA.
This document provides information about genetic code. It defines genetic code as the set of rules by which DNA and RNA sequences are translated into proteins. The genetic code is made up of 64 codons consisting of three nucleotides each. 61 codons code for 20 amino acids while 3 are termination codons. The genetic code is expressed in a table mapping the 64 codons to their corresponding amino acids or termination signal. The document also discusses anticodons, which are sequences in tRNA that pair with mRNA codons during protein translation.
The document discusses the genetic code, which is a set of rules that specifies how sequences of nucleotides in DNA and RNA are translated into proteins. It notes that the genetic code is universal, uses triplets of nucleotides (codons), and has some level of degeneracy whereby more than one codon can code for an amino acid. This redundancy is explained by Crick's wobble hypothesis regarding base pairing at the third position of codons and anticodons.
This document discusses proteins and was written by Dr. Kayeen Vadakkan, an assistant professor from St. Mary's College Thrissur, Kerala, India. It covers the classification, structure, and functions of proteins. Proteins can be classified based on their function, chemical nature and solubility, and nutritional properties. The structure of proteins includes primary, secondary, tertiary, and quaternary levels. Primary structure is the amino acid sequence, secondary involves folding patterns like alpha helices and beta sheets, tertiary is the three-dimensional structure, and quaternary involves interactions of subunits.
This document discusses amino acids, which are organic compounds that contain amino and carboxyl groups and form proteins by binding together via peptide bonds. Amino acids are classified based on their structure, polarity, and nutritional requirements. There are essential and non-essential amino acids. Amino acids can undergo reactions like decarboxylation, amide formation, transamination, and oxidative deamination. They have amphoteric properties due to acidic and basic groups and exist as zwitterions at their isoelectric pH. Peptide bonds between amino acids are planar and rigid.
1. Nucleic acids consist of nitrogen bases, pentose sugars, and phosphates. The pentose sugar is D-ribose in RNA and 2-deoxy D-ribose in DNA.
2. Purine nucleotides are synthesized through a de novo pathway where inosine monophosphate (IMP) is synthesized from basic building blocks like aspartate, glycine, and glutamine and later converted to AMP and GMP.
3. Pyrimidine nucleotides are synthesized by first forming orotidine monophosphate from aspartate, carbamoyl phosphate, and glutamine, which is then converted to UMP and other pyrimidine nucleotides.
The complement system is a collection of circulating and cell membrane proteins that play important roles in host defense against microbes and in antibody mediated tissue injury. It has three major pathways of activation - the classical, alternative, and lectin pathways. Activation leads to the generation of effector molecules that help eliminate microbes through lysis, opsonization, and inflammation. Deficiencies in complement components increase susceptibility to certain bacterial and viral infections as well as immune complex diseases.
Cytokines are proteins that mediate communication between cells to coordinate the immune response. They are secreted by white blood cells and other cells in response to stimuli. Cytokines help regulate immune cell development and function, inducing inflammatory responses, hematopoiesis, cell proliferation and differentiation, and wound healing. They signal through high affinity receptors via autocrine, paracrine, or endocrine actions and exhibit pleiotropy, redundancy, synergy, and antagonism. Cytokines are classified into families including hematopoietins, chemokines, interferons, TNF, and CSFs. TH1 and TH2 cells secrete different cytokine profiles that determine immune response type. Cytokine antagonists and inhibitors regulate cytokine activity.
1. The MHC molecules present peptide antigens to T cells. Class I MHC present intracellular peptides to CD8+ T cells, while class II MHC present extracellular peptides taken up by endocytosis to CD4+ T cells.
2. Antigens are processed through different pathways depending on if they are intracellular or extracellular. Intracellular antigens are degraded by the proteasome and transported into the ER by TAP to bind class I MHC. Extracellular antigens are endocytosed and degraded in lysosomes to bind class II MHC.
3. The peptide-MHC complexes are then transported to the cell surface for recognition by T cell receptors.
The document summarizes two pathways - the hexose monophosphate (HMP) pathway and the uronic acid pathway. The HMP pathway, also known as the pentose phosphate pathway, generates pentoses and NADPH through oxidative and non-oxidative phases involving multiple enzyme-catalyzed reactions. The uronic acid pathway is an alternative oxidative pathway for glucose that results in the synthesis of glucuronic acid, pentoses, and vitamin C, through a series of four phases including the formation of UDP-glucuronate and its conversion to L-gulonate.
Gluconeogenesis and glycogenolysis are pathways that produce glucose. Gluconeogenesis produces glucose from non-carbohydrate precursors mainly in the liver. Glycogenolysis breaks down glycogen stores in the liver and muscle into glucose-1-phosphate and free glucose. Glycogenesis is the synthesis of glycogen from glucose using UDP-glucose and glycogenin to initiate glycogen synthesis and form branched glycogen structures through the actions of glycogen synthase and branching enzyme.
The citric acid cycle is the key metabolic pathway that generates energy in the form of ATP and NADH through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The cycle's 10 steps occur in the mitochondrial matrix and involve enzymatic conversions between citrate, isocitrate, alpha-ketoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate. Two carbon atoms are removed as CO2 from acetyl-CoA in each turn of the cycle, generating high-energy electron carriers used in oxidative phosphorylation to produce ATP.
This document discusses glycolysis, the pathway that breaks down glucose to pyruvate. Glycolysis occurs in the cytosol of cells and can proceed with or without oxygen. It is an important pathway for ATP generation. The document outlines the 10 steps of glycolysis, including an energy investment phase where ATP is used to phosphorylate glucose, and an energy generation phase where ATP is regenerated. Phosphofructokinase is identified as the rate-limiting step. The fate of pyruvate, the end product, depends on oxygen availability, leading to aerobic or anaerobic metabolism.
Mechanism of vd(j) recombination and generation of antibody diversityKayeen Vadakkan
The document summarizes the mechanism of V(D)J recombination and generation of antibody diversity. It discusses:
1) How V(D)J recombination involves rearrangement of one V, D (only in heavy chains), and J gene segment in B and T lymphocytes, bringing them under the control of regulatory elements.
2) The recognition signals and rearrangement process, which involves double stranded breaks and joining of coding ends.
3) The four main stages of V(D)J recombination - synapsis, cleavage, hairpin opening and end processing, and joining.
4) The seven means by which antibody diversity is generated - multiple gene segments, combinatorial joining, junctional flexibility
1. The document discusses the multigene organization of immunoglobulins, including the lambda and kappa light chains and heavy chains.
2. It describes how each contains multiple gene segments (V, D, J, C) that rearrange during B cell maturation to generate the variable and constant regions that determine antibody specificity.
3. The gene segments are located on different chromosomes and rearrangement of V, D, J segments in heavy chains and V, J segments in light chains creates enormous antibody diversity.
Cholesterol is a structural component of cell membranes and is a precursor for other steroids like hormones and vitamin D. It is essential for the structure of lipoproteins which transport lipids throughout the body, including transporting fatty acids to the liver bound to cholesteryl esters for breakdown.
1. Fatty acids in the body undergo beta-oxidation, where they are sequentially broken down into two-carbon acetyl-CoA units through four reactions: oxidation, hydration, oxidation, and cleavage.
2. Beta-oxidation involves three stages: activation of fatty acids into acyl-CoA in the cytosol, transport of acyl-CoA into the mitochondria via the carnitine shuttle system, and beta-oxidation proper within the mitochondrial matrix.
3. Each round of beta-oxidation liberates one acetyl-CoA molecule through a cycle of oxidation, hydration, further oxidation, and thiolytic cleavage of the acyl-CoA.
Biosynthesis of fatty acids occurs predominantly in the liver, kidney, adipose tissue and mammary glands. Acetyl CoA and NADPH provide the building blocks and reducing power for fatty acid formation. Fatty acid synthesis occurs in three stages: 1) Acetyl CoA and NADPH are produced in the mitochondria and cytosol, respectively; 2) Acetyl CoA is carboxylated to malonyl CoA by acetyl CoA carboxylase; 3) The fatty acid synthase complex catalyzes the reactions to elongate the fatty acid chain by two carbons at a time using malonyl CoA, producing a longer fatty acid with each cycle.
Enzymes are catalysts that accelerate biochemical reactions by lowering the activation energy. They do this by binding to substrates in their active site, which releases energy and activates the substrates. The lock and key model proposes a perfect fit between enzyme and substrate shapes. The induced fit model suggests some flexibility in the active site. Enzymes bind substrates via various bonds like ionic, hydrogen, and Van der Waals. Allosteric enzymes have additional effector binding sites that cause conformational changes altering activity. Isozymes are enzymes that catalyze the same reaction but differ in structure and properties. Ribozymes are catalytically active RNA molecules.
The document summarizes the urea cycle, which occurs in the liver to convert ammonia into urea for excretion. It involves several steps spanning the mitochondria and cytosol. Carbamoyl phosphate synthetase activates ammonia and CO2 to initiate the cycle. Ornithine, aspartate, and several other compounds join the cycle through condensation reactions requiring ATP. Arginase produces urea and ornithine at the end of the cycle. The cycle is connected to the Krebs cycle and regulated by factors like dietary protein and N-acetyl glutamate. Deficiencies in cycle enzymes can cause diseases with high ammonia levels like hyperammonemia.
The document discusses the three main types of RNA: messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). mRNA carries copies of instructions from DNA to the ribosome and acts as a messenger between DNA and protein synthesis. rRNA combines with proteins to form ribosomes, which are the sites of protein synthesis. tRNA transfers amino acids to the growing polypeptide chain during protein translation and acts as an adapter between mRNA and amino acids.
The document summarizes the pentose phosphate pathway. It consists of an oxidative phase and a non-oxidative phase. The oxidative phase generates NADPH and ribulose 5-phosphate through oxidation reactions. The non-oxidative phase converts ribulose 5-phosphate into other 5-carbon sugars, regenerating glucose 6-phosphate while producing ribose 5-phosphate. The pathway provides reducing power in the form of NADPH for biosynthesis and maintains levels of the antioxidant glutathione.
The document provides an overview of nitrogen metabolism. It discusses (1) the importance of nitrogen in proteins and nucleic acids, (2) the key anabolic processes of nitrogen fixation, amino acid synthesis and protein synthesis, and (3) the main catabolic processes of proteolysis, nitrification and denitrification. Nitrogen is obtained from the atmosphere through nitrogen fixation by bacteria and is used to synthesize amino acids and proteins essential for plant structure and function.
The chapter Lifelines of National Economy in Class 10 Geography focuses on the various modes of transportation and communication that play a vital role in the economic development of a country. These lifelines are crucial for the movement of goods, services, and people, thereby connecting different regions and promoting economic activities.
A Visual Guide to 1 Samuel | A Tale of Two HeartsSteve Thomason
These slides walk through the story of 1 Samuel. Samuel is the last judge of Israel. The people reject God and want a king. Saul is anointed as the first king, but he is not a good king. David, the shepherd boy is anointed and Saul is envious of him. David shows honor while Saul continues to self destruct.
This presentation was provided by Racquel Jemison, Ph.D., Christina MacLaughlin, Ph.D., and Paulomi Majumder. Ph.D., all of the American Chemical Society, for the second session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session Two: 'Expanding Pathways to Publishing Careers,' was held June 13, 2024.
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...PECB
Denis is a dynamic and results-driven Chief Information Officer (CIO) with a distinguished career spanning information systems analysis and technical project management. With a proven track record of spearheading the design and delivery of cutting-edge Information Management solutions, he has consistently elevated business operations, streamlined reporting functions, and maximized process efficiency.
Certified as an ISO/IEC 27001: Information Security Management Systems (ISMS) Lead Implementer, Data Protection Officer, and Cyber Risks Analyst, Denis brings a heightened focus on data security, privacy, and cyber resilience to every endeavor.
His expertise extends across a diverse spectrum of reporting, database, and web development applications, underpinned by an exceptional grasp of data storage and virtualization technologies. His proficiency in application testing, database administration, and data cleansing ensures seamless execution of complex projects.
What sets Denis apart is his comprehensive understanding of Business and Systems Analysis technologies, honed through involvement in all phases of the Software Development Lifecycle (SDLC). From meticulous requirements gathering to precise analysis, innovative design, rigorous development, thorough testing, and successful implementation, he has consistently delivered exceptional results.
Throughout his career, he has taken on multifaceted roles, from leading technical project management teams to owning solutions that drive operational excellence. His conscientious and proactive approach is unwavering, whether he is working independently or collaboratively within a team. His ability to connect with colleagues on a personal level underscores his commitment to fostering a harmonious and productive workplace environment.
Date: May 29, 2024
Tags: Information Security, ISO/IEC 27001, ISO/IEC 42001, Artificial Intelligence, GDPR
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Beyond Degrees - Empowering the Workforce in the Context of Skills-First.pptxEduSkills OECD
Iván Bornacelly, Policy Analyst at the OECD Centre for Skills, OECD, presents at the webinar 'Tackling job market gaps with a skills-first approach' on 12 June 2024
1. Genetic Code
By,
Dr. Kayeen Vadakkan
Assistant Professor,
Department of Biotechnology
St. Mary's College Thrissur,
Kerala , India
2. Topics Covered
• Genetic Code
• Discovery of Genetic Code
• Characteristics of Genetic code
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
3. Genetic Code
Definition
The genetic code is a triplet of nucleotides that codes for a
specific amino acid.
A U A C G A G U C
Triplet Codon
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
4. Discovery of genetic code
The discovery of genetic code and translation was based on the
experiments and observations made by three independent group
of scientists.
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
5. Discovery 1
In 1950, Paul Zamecnik and
his team discovered that the
site of protein synthesis is
ribosomes
Discovery 2
Mahlon Hoagland and Paul
Zamecnik discovered that
the amino acids are activated
when incubated with ATPs
Discovery 3
Francis Crik discovered that
how genetic informations are
coded in 4 letter language
(ATGC)
A nucleic acid can function
as adaptor where in one part
bind with amino acid and
one with mRNA.
Genetic Code
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
6. Characteristics of genetic code
1. Translation occurs when genetic code is read in successive ,
non overlapping way
There is a possibility that the genetic code may be read in either over lapping manner or
non over lapping manner
A U A C G A
1
2
3
Overlapping Code
A U A C G A
1 2
Non- Overlapping Code
In overlapping code same nucleotide in mRNA will be shared by different codon, however in
non-overlapping codon nucleotides are not shared by codon.
In all living organisms the genetic code is non-overlapping
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
7. Characteristics of genetic code
(Continues)2. Reading frame of Genetic Code
It is the specific first codon in a mRNA sequence.
A new codon begins at each three nucleotide residue
There is no punctuation between these triplet codons
The amino acid sequence is determined by the linear sequence of continuous triplets.
There is a possibility that in a single mRNA shall have various reading frame
U U C U C G G A C
U U C U C G G A C
U U C U C G G A C
Reading Frame I
Reading Frame II
Reading Frame III
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
8. Characteristics of genetic code
(Continues)3. 64 Triplet Codons
There are total 64 triplet codons present in mRNA
Termination Codon : The termination codon UAA, UAG, UGA are also called as the stop
codons/Non-sense codon.
They stop the synthesis of amino acids and does not code for any known amino acids.
In general in a reading frame one in every 20 codons will be a termination codon
Initiation Codon : The initiation codon (AUG) are the common signal for the beginning of
protein synthesis.
Open Reading Frame : A reading frame without a termination codon for fifty or more
codons are referred as open reading frame
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
9. Characteristics of genetic code
(Continues)4. Degeneracy of Genetic Code
Definition
The phenomenon through which a single amino acid may be specified by more than one
codon is called the degeneracy of genetic code.
The degeneracy of genetic code is not uniform
Example : there are 6 different codons present in mRNA that codes for Arginine, three
codons for Isoleucine and only one codon for Methionine
UC G
CC G
AC G
GC G
GA A
GGA
Arginine
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur
10. Further reading
1. Lehninger Principles of Biochemistry by Michael M Cox and David L Nelson
2. Molecular Biology of the Genes – J.D.Watson, N.H.Hopkins
3. Moleculary Cell Biology, J.Darnell, H.Lodish
4. Gene VIII, Benjamin Lewin
5. Genomes, T.S.Brown
6. Molecular Cloning: a Laboratory Manual, J.Sambrook.
Molecular Biology, Kayeen Vadakkan, Department of Biotechnology, St. Mary's College, Thrissur