I have tried to make a precise presentation on protein transport, targeting and sorting into organelle's other than nucleus. Hope this might help you. Comments are welcome.
Mitochondria contain proteins encoded by both their own genome and the nuclear genome. Newly synthesized nuclear-encoded proteins contain targeting signals that direct them to the mitochondria. There are several pathways that transport mitochondrial proteins across the outer and inner membranes and sort them to their correct submitochondrial compartment - the outer membrane, intermembrane space, inner membrane, or matrix. Protein translocases like TOM, TIM23, and TIM22 recognize different targeting signals and mediate the transport and sorting of precursor proteins to their proper destinations.
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.
The delivery of newly synthesized protein to their proper cellular destination, usually referred to as protein targeting or sorting.
The mode of protein transport depends chiefly on the location in the cell cytoplasm of the polysomes involved in protein synthesis.
There are two modes of protein sorting:-
1) Co - translational Transportation.
2) Post - translational Transportation.
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.
Synthesis and targeting of mitochondrial proteinsPrachee Rajput
Mitochondrial proteins are essential for processes like oxidative phosphorylation and ATP synthesis. They are synthesized on cytosolic ribosomes and targeted to mitochondria. The precursor proteins contain an N-terminal targeting sequence that binds receptor proteins on the mitochondrial surface. The precursor proteins then pass through membrane channels into the mitochondrial matrix, where the targeting sequence is cleaved off and the proteins fold with the help of chaperones. This import process is tightly regulated and requires coordination between the nuclear and mitochondrial genomes.
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 nuclear structure and transport. It discusses that the nucleus contains DNA and is surrounded by a double membrane nuclear envelope containing pores. It also contains non-membrane bound subcompartments like the nucleolus. Chromosomes occupy distinct territories in the nucleus. Large molecules are transported between the nucleus and cytoplasm through nuclear pores using nuclear import and export sequences. RNAs and ribosomal subunits use specific export receptors to move through the pores.
I have tried to make a precise presentation on protein transport, targeting and sorting into organelle's other than nucleus. Hope this might help you. Comments are welcome.
Mitochondria contain proteins encoded by both their own genome and the nuclear genome. Newly synthesized nuclear-encoded proteins contain targeting signals that direct them to the mitochondria. There are several pathways that transport mitochondrial proteins across the outer and inner membranes and sort them to their correct submitochondrial compartment - the outer membrane, intermembrane space, inner membrane, or matrix. Protein translocases like TOM, TIM23, and TIM22 recognize different targeting signals and mediate the transport and sorting of precursor proteins to their proper destinations.
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.
The delivery of newly synthesized protein to their proper cellular destination, usually referred to as protein targeting or sorting.
The mode of protein transport depends chiefly on the location in the cell cytoplasm of the polysomes involved in protein synthesis.
There are two modes of protein sorting:-
1) Co - translational Transportation.
2) Post - translational Transportation.
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.
Synthesis and targeting of mitochondrial proteinsPrachee Rajput
Mitochondrial proteins are essential for processes like oxidative phosphorylation and ATP synthesis. They are synthesized on cytosolic ribosomes and targeted to mitochondria. The precursor proteins contain an N-terminal targeting sequence that binds receptor proteins on the mitochondrial surface. The precursor proteins then pass through membrane channels into the mitochondrial matrix, where the targeting sequence is cleaved off and the proteins fold with the help of chaperones. This import process is tightly regulated and requires coordination between the nuclear and mitochondrial genomes.
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 nuclear structure and transport. It discusses that the nucleus contains DNA and is surrounded by a double membrane nuclear envelope containing pores. It also contains non-membrane bound subcompartments like the nucleolus. Chromosomes occupy distinct territories in the nucleus. Large molecules are transported between the nucleus and cytoplasm through nuclear pores using nuclear import and export sequences. RNAs and ribosomal subunits use specific export receptors to move through the pores.
Protein targeting or protein sorting is the mechanism by which a cell transports to the appropriate positions in the cell or outside of it. Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to a specific sub-cellular location or exported from the cell for correct activity. This phenomenon is called protein targeting. Protein targeting is necessary for proteins that are destined to work outside the cytoplasm.This delivery process is carried out based on information contained in the protein itself. Correct sorting is crucial for the cell; errors can lead to diseases. In 1970, Günter Blobel conducted experiments on the translocation of proteins across membranes. He was awarded the 1999 Nobel Prize for his findings. He discovered that many proteins have a signal sequence, that is, a short amino acid sequence at one end that functions like a postal code for the target organelle.
Transcription in prokaryotes involves RNA polymerase producing messenger RNA transcripts of genetic material in the cytoplasm. Unlike in eukaryotes, transcription and translation can occur simultaneously. Transcription is controlled by transcription factors and involves three main steps: initiation, elongation, and termination. Initiation requires RNA polymerase binding to promoter regions with sigma factors. Elongation adds complementary bases to the DNA template. Termination can occur via intrinsic terminator sequences forming stem-loop structures or with rho-dependent termination using a rho factor protein.
Protein Import & Mitochondrial AssemblyAnkit Alankar
This document discusses protein import into mitochondria. It describes how most mitochondrial proteins are synthesized in the cytosol and contain targeting sequences that direct their import through translocases in the outer and inner mitochondrial membranes. The Tom complex handles transport across the outer membrane, while the Tim23 complex mediates import through the inner membrane. Molecular chaperones maintain imported proteins in an unfolded state as they pass through the translocases with the help of membrane potentials.
Post translational modification of proteincoolsid13
The document discusses various types of post-translational modifications (PTMs) of proteins. It describes how PTMs are necessary for normal protein functioning by affecting stability, activity, localization, and signaling. It provides examples of common PTMs like phosphorylation, glycosylation, acetylation, lipidation, disulfide bonding, and ubiquitination. It also discusses protein folding, subunit aggregation, and protein splicing - key processes in protein maturation that occur after translation. PTMs are an important mechanism for regulating protein structure and function after synthesis.
Translation is the process by which proteins are synthesized from messenger RNA (mRNA) in eukaryotes, which are organisms with membrane-bound nuclei. Translation involves mRNA being decoded on ribosomes into a polypeptide chain. It occurs through three main steps - initiation, elongation, and termination. Initiation involves the small ribosomal subunit binding to the 5' end of mRNA and scanning for the start codon. Elongation is the sequential addition of amino acids specified by the mRNA codons. Termination occurs when a stop codon is reached and release factors cause the ribosome to dissociate and release the completed protein.
One of the first plausible models to account for the preceding observations was
formulated by Robin Holliday.
The key features of the Holliday model are the formation of heteroduplex DNA; the
creation of a cross bridge; its migration along the two heteroduplex strands,
termed branch migration; the occurrence of mismatch repair; and the
subsequent resolution, or splicing, of the intermediate structure to yield different
typesof recombinant molecules.
This document discusses different types of chaperone proteins. It begins by explaining that chaperones assist other proteins in folding correctly by interacting with unfolded or misfolded proteins. The main types discussed are molecular chaperones like Hsp70 and Hsp90, and chaperonins. Hsp70 binds to hydrophobic regions of unfolded proteins to prevent aggregation, while Hsp90 helps activate client proteins. Chaperonins form folding chambers and there are two groups - group 1 found in prokaryotes and organelles, and group 2 in eukaryotes and archaea. Specific examples of chaperone homologs in different organisms are also provided.
This document discusses the C-Value Paradox, which is the observation that there is no correlation between the complexity of an organism and the amount of DNA (C-value) in its genome. The document provides examples showing that C-values, or the amount of DNA per haploid cell, can vary widely both within and across species, from 105 base pairs in mycoplasma to over 109 base pairs in mammals. While complexity tends to increase with higher C-values, exceptions exist, demonstrating there is no direct linear relationship between genome size and organism complexity. The term "C-value" refers to the haploid DNA content of a species.
This document discusses chloroplast DNA (cpDNA). Chloroplasts contain their own circular genome of double-stranded DNA ranging from 140-200kb. The cpDNA contains genes that code for proteins involved in photosynthesis as well as rRNA and tRNA. It has a quadripartite structure containing single copy and inverted repeat regions. Tobacco and liverwort were two of the first chloroplast genomes to be sequenced. Molecular studies of cpDNA regions have been useful for plant systematics. Replication of cpDNA is independent of nuclear DNA and involves enzymes like DNA polymerase and helicase.
The document discusses protein sorting in Golgi bodies. It describes how proteins are modified and sorted as they pass through the cis, medial, and trans faces of the Golgi apparatus. Proteins undergo processing like glycosylation and are targeted to their final destinations, such as organelles, vesicles, or secretion. The Golgi apparatus plays a key role in modifying and sorting proteins to their correct locations within and outside the cell.
Introduction
Protein modifications
Folding
Chaperon mediated
Enzymatic
Cleavage
Addition of functional groups
Chemical groups
Hydrophobic groups
Proteolysis
Conclusion
Reference
Chloroplasts are organelles found in plant cells and algae that conduct photosynthesis. They contain their own DNA known as the chloroplast genome, which is typically 100-200kb in size and encodes genes for photosynthesis. The chloroplast genome is highly conserved and maternally inherited. It has been used for phylogenetic studies and shows potential for genetic engineering due to high transgene expression and maternal inheritance that prevents gene flow to other species.
Basics of Undergraduate/university fellows
Transcription is more complicated in eukaryotes than in prokaryotes because
eukaryotes possess three different classes of RNA polymerases and because of the
way in which transcripts are processed to their functional forms.
More proteins and transcription factors are involved in eukaryotic transcription.
This document summarizes the process of nuclear export of messenger RNA (mRNA). It begins with an introduction describing how mRNA must be exported from the nucleus to the cytoplasm to be translated into protein. It then discusses the importance of nuclear export and describes the nuclear pore complex that facilitates transport. The document outlines the roles of Ran GTPase and transport receptors in nuclear export. It provides details on the adaptor-receptor system and multistep process of mRNA export, including recruitment of export factors, translocation through the nuclear pore, and release into the cytoplasm. The summary concludes with sections on regulation and quality control of mRNA export.
transcription activators, repressors, & control RNA splicing, procesing and e...ranjithahb ranjithahbhb
RNA processing involves several steps to convert primary transcripts into mature mRNA in eukaryotic cells. These include 5' capping, 3' cleavage and polyadenylation, and RNA splicing. RNA splicing involves two transesterification reactions that remove introns and join exons. Alternative splicing allows a single gene to produce multiple protein variants. Eukaryotic gene expression is regulated by transcriptional activators and repressors that bind cis-regulatory elements like promoters and enhancers. Activators recruit transcriptional machinery while repressors inhibit transcription. Chromatin structure also influences transcription with acetylation associated with active genes.
1) Eukaryotic gene expression is regulated at multiple levels including transcription, chromatin structure, post-transcriptional processing, and translation.
2) Regulation allows for adaptation and tissue-specific gene expression during development. Key differences from prokaryotes include the lack of operons and more complex regulation in eukaryotes.
3) Gene expression can be regulated short-term through transcriptional control, as seen in yeast galactose-utilizing genes, or long-term for development through mechanisms like chromatin remodeling.
This document discusses transposable elements (TEs), which are segments of DNA that can change positions within the genome. It classifies TEs into two classes based on their mechanism of transposition. Class 1 elements use a "cut and paste" mechanism involving transposase, while Class 2 retrotransposons use reverse transcriptase in a "copy and paste" mechanism. Examples of TEs discussed include Ac-Ds elements in maize, P elements in Drosophila, and LINEs and SINEs in humans. The effects of TE insertion include gene mutation, changes in gene regulation, gene duplication, deletion, and chromosome rearrangements. Applications of TEs include their use as cloning vectors and providing raw material for evolution
Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to their correct subcellular locations. Secretory proteins have an N-terminal signal peptide that targets them to the endoplasmic reticulum, where they are translocated and modified. Transport vesicles then carry proteins from the ER to the Golgi complex for further modification. From the Golgi, vesicles transport proteins either to other organelles or fuse with the plasma membrane to release proteins outside the cell. Correct protein targeting and trafficking is essential for cellular function.
Intracellular trafficking and protein sortingapeksha40
This document discusses intracellular protein trafficking and sorting. It describes how proteins contain signal sequences that target them to different organelles like the endoplasmic reticulum, mitochondria, peroxisomes and nucleus. It explains the roles of the signal recognition particle, translocon complex and chaperones in transporting proteins into the ER. The Ran GTPase system and importins/exportins are also summarized in their role in nuclear transport. Clinical implications of defects in peroxisome biogenesis are mentioned.
Protein targeting or protein sorting is the mechanism by which a cell transports to the appropriate positions in the cell or outside of it. Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to a specific sub-cellular location or exported from the cell for correct activity. This phenomenon is called protein targeting. Protein targeting is necessary for proteins that are destined to work outside the cytoplasm.This delivery process is carried out based on information contained in the protein itself. Correct sorting is crucial for the cell; errors can lead to diseases. In 1970, Günter Blobel conducted experiments on the translocation of proteins across membranes. He was awarded the 1999 Nobel Prize for his findings. He discovered that many proteins have a signal sequence, that is, a short amino acid sequence at one end that functions like a postal code for the target organelle.
Transcription in prokaryotes involves RNA polymerase producing messenger RNA transcripts of genetic material in the cytoplasm. Unlike in eukaryotes, transcription and translation can occur simultaneously. Transcription is controlled by transcription factors and involves three main steps: initiation, elongation, and termination. Initiation requires RNA polymerase binding to promoter regions with sigma factors. Elongation adds complementary bases to the DNA template. Termination can occur via intrinsic terminator sequences forming stem-loop structures or with rho-dependent termination using a rho factor protein.
Protein Import & Mitochondrial AssemblyAnkit Alankar
This document discusses protein import into mitochondria. It describes how most mitochondrial proteins are synthesized in the cytosol and contain targeting sequences that direct their import through translocases in the outer and inner mitochondrial membranes. The Tom complex handles transport across the outer membrane, while the Tim23 complex mediates import through the inner membrane. Molecular chaperones maintain imported proteins in an unfolded state as they pass through the translocases with the help of membrane potentials.
Post translational modification of proteincoolsid13
The document discusses various types of post-translational modifications (PTMs) of proteins. It describes how PTMs are necessary for normal protein functioning by affecting stability, activity, localization, and signaling. It provides examples of common PTMs like phosphorylation, glycosylation, acetylation, lipidation, disulfide bonding, and ubiquitination. It also discusses protein folding, subunit aggregation, and protein splicing - key processes in protein maturation that occur after translation. PTMs are an important mechanism for regulating protein structure and function after synthesis.
Translation is the process by which proteins are synthesized from messenger RNA (mRNA) in eukaryotes, which are organisms with membrane-bound nuclei. Translation involves mRNA being decoded on ribosomes into a polypeptide chain. It occurs through three main steps - initiation, elongation, and termination. Initiation involves the small ribosomal subunit binding to the 5' end of mRNA and scanning for the start codon. Elongation is the sequential addition of amino acids specified by the mRNA codons. Termination occurs when a stop codon is reached and release factors cause the ribosome to dissociate and release the completed protein.
One of the first plausible models to account for the preceding observations was
formulated by Robin Holliday.
The key features of the Holliday model are the formation of heteroduplex DNA; the
creation of a cross bridge; its migration along the two heteroduplex strands,
termed branch migration; the occurrence of mismatch repair; and the
subsequent resolution, or splicing, of the intermediate structure to yield different
typesof recombinant molecules.
This document discusses different types of chaperone proteins. It begins by explaining that chaperones assist other proteins in folding correctly by interacting with unfolded or misfolded proteins. The main types discussed are molecular chaperones like Hsp70 and Hsp90, and chaperonins. Hsp70 binds to hydrophobic regions of unfolded proteins to prevent aggregation, while Hsp90 helps activate client proteins. Chaperonins form folding chambers and there are two groups - group 1 found in prokaryotes and organelles, and group 2 in eukaryotes and archaea. Specific examples of chaperone homologs in different organisms are also provided.
This document discusses the C-Value Paradox, which is the observation that there is no correlation between the complexity of an organism and the amount of DNA (C-value) in its genome. The document provides examples showing that C-values, or the amount of DNA per haploid cell, can vary widely both within and across species, from 105 base pairs in mycoplasma to over 109 base pairs in mammals. While complexity tends to increase with higher C-values, exceptions exist, demonstrating there is no direct linear relationship between genome size and organism complexity. The term "C-value" refers to the haploid DNA content of a species.
This document discusses chloroplast DNA (cpDNA). Chloroplasts contain their own circular genome of double-stranded DNA ranging from 140-200kb. The cpDNA contains genes that code for proteins involved in photosynthesis as well as rRNA and tRNA. It has a quadripartite structure containing single copy and inverted repeat regions. Tobacco and liverwort were two of the first chloroplast genomes to be sequenced. Molecular studies of cpDNA regions have been useful for plant systematics. Replication of cpDNA is independent of nuclear DNA and involves enzymes like DNA polymerase and helicase.
The document discusses protein sorting in Golgi bodies. It describes how proteins are modified and sorted as they pass through the cis, medial, and trans faces of the Golgi apparatus. Proteins undergo processing like glycosylation and are targeted to their final destinations, such as organelles, vesicles, or secretion. The Golgi apparatus plays a key role in modifying and sorting proteins to their correct locations within and outside the cell.
Introduction
Protein modifications
Folding
Chaperon mediated
Enzymatic
Cleavage
Addition of functional groups
Chemical groups
Hydrophobic groups
Proteolysis
Conclusion
Reference
Chloroplasts are organelles found in plant cells and algae that conduct photosynthesis. They contain their own DNA known as the chloroplast genome, which is typically 100-200kb in size and encodes genes for photosynthesis. The chloroplast genome is highly conserved and maternally inherited. It has been used for phylogenetic studies and shows potential for genetic engineering due to high transgene expression and maternal inheritance that prevents gene flow to other species.
Basics of Undergraduate/university fellows
Transcription is more complicated in eukaryotes than in prokaryotes because
eukaryotes possess three different classes of RNA polymerases and because of the
way in which transcripts are processed to their functional forms.
More proteins and transcription factors are involved in eukaryotic transcription.
This document summarizes the process of nuclear export of messenger RNA (mRNA). It begins with an introduction describing how mRNA must be exported from the nucleus to the cytoplasm to be translated into protein. It then discusses the importance of nuclear export and describes the nuclear pore complex that facilitates transport. The document outlines the roles of Ran GTPase and transport receptors in nuclear export. It provides details on the adaptor-receptor system and multistep process of mRNA export, including recruitment of export factors, translocation through the nuclear pore, and release into the cytoplasm. The summary concludes with sections on regulation and quality control of mRNA export.
transcription activators, repressors, & control RNA splicing, procesing and e...ranjithahb ranjithahbhb
RNA processing involves several steps to convert primary transcripts into mature mRNA in eukaryotic cells. These include 5' capping, 3' cleavage and polyadenylation, and RNA splicing. RNA splicing involves two transesterification reactions that remove introns and join exons. Alternative splicing allows a single gene to produce multiple protein variants. Eukaryotic gene expression is regulated by transcriptional activators and repressors that bind cis-regulatory elements like promoters and enhancers. Activators recruit transcriptional machinery while repressors inhibit transcription. Chromatin structure also influences transcription with acetylation associated with active genes.
1) Eukaryotic gene expression is regulated at multiple levels including transcription, chromatin structure, post-transcriptional processing, and translation.
2) Regulation allows for adaptation and tissue-specific gene expression during development. Key differences from prokaryotes include the lack of operons and more complex regulation in eukaryotes.
3) Gene expression can be regulated short-term through transcriptional control, as seen in yeast galactose-utilizing genes, or long-term for development through mechanisms like chromatin remodeling.
This document discusses transposable elements (TEs), which are segments of DNA that can change positions within the genome. It classifies TEs into two classes based on their mechanism of transposition. Class 1 elements use a "cut and paste" mechanism involving transposase, while Class 2 retrotransposons use reverse transcriptase in a "copy and paste" mechanism. Examples of TEs discussed include Ac-Ds elements in maize, P elements in Drosophila, and LINEs and SINEs in humans. The effects of TE insertion include gene mutation, changes in gene regulation, gene duplication, deletion, and chromosome rearrangements. Applications of TEs include their use as cloning vectors and providing raw material for evolution
Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to their correct subcellular locations. Secretory proteins have an N-terminal signal peptide that targets them to the endoplasmic reticulum, where they are translocated and modified. Transport vesicles then carry proteins from the ER to the Golgi complex for further modification. From the Golgi, vesicles transport proteins either to other organelles or fuse with the plasma membrane to release proteins outside the cell. Correct protein targeting and trafficking is essential for cellular function.
Intracellular trafficking and protein sortingapeksha40
This document discusses intracellular protein trafficking and sorting. It describes how proteins contain signal sequences that target them to different organelles like the endoplasmic reticulum, mitochondria, peroxisomes and nucleus. It explains the roles of the signal recognition particle, translocon complex and chaperones in transporting proteins into the ER. The Ran GTPase system and importins/exportins are also summarized in their role in nuclear transport. Clinical implications of defects in peroxisome biogenesis are mentioned.
Protein merged (Dr Addis)-430-686-1-150.pdfGashawDesta2
Proteins can be localized either post-translationally or co-translationally. Post-translationally localized proteins are released into the cytosol after synthesis on free ribosomes and may then be targeted to organelles like the nucleus or mitochondria. Co-translationally localized proteins associate with the ER membrane during synthesis, so their ribosomes are membrane-bound. These proteins pass into the ER and travel through the Golgi apparatus and plasma membrane unless retained at an earlier step. Signal sequences on proteins initiate their co-translational translocation and contain a central hydrophobic region flanked by polar residues.
best pdf for molecular biology Protein.pdfGashawDesta2
Proteins can be localized either post-translationally or co-translationally. Post-translationally synthesized proteins are released into the cytosol after synthesis on free ribosomes and some have targeting signals to direct them to organelles like the nucleus or mitochondria. Co-translationally localized proteins associate with the ER membrane during synthesis, so their ribosomes are membrane-bound. These proteins pass into the ER and follow the secretory pathway through the Golgi apparatus and plasma membrane, unless they have retention signals. Proteins enter organelles through translocation complexes that allow passage across membranes without exposure to the hydrophobic lipid bilayer.
A comparative study using different measure of filterationpurkaitjayati29
This document presents a study comparing different scoring functions used in filter-based feature selection methods for microarray gene expression data. Chapter 1 introduces gene expression, DNA microarrays, and the goals of classification and feature selection. Chapter 2 provides background on bioinformatics, molecular biology, and the central dogma. Chapter 3 describes DNA microarray technology and gene expression data. Chapter 4 reviews literature on feature selection techniques applied to microarray data, discussing filter, wrapper, embedded, hybrid, and ensemble methods. Chapter 5 proposes using a scoring function-based filter method to select relevant genes, focusing on mutual information, symmetric uncertainty, information gain, and Chi-square scoring functions.
Protein sorting and transport to lysosomesRamaJumwal2
Protein sorting is the mechanism by which cells transport proteins to their proper subcellular locations. Newly synthesized proteins must be delivered to specific destinations for correct function. This delivery process uses targeting signals contained within the protein sequences. There are two main pathways for protein targeting - post-translational translocation where proteins are transported after synthesis, and co-translational translocation where proteins are transferred to the endoplasmic reticulum during synthesis. Targeting signals include signal peptides and presequences that enable the transport machinery to correctly position proteins inside or outside the cell.
How are proteins imported into the thylakoids of chloroplastsSo.pdffootwearpark
How are proteins imported into the thylakoids of chloroplasts?
Solution
Answer:
Nuclear-encoded thylakoid proteins are first imported into the chloroplast and then directed to
the thylakoid using different sorting mechanisms.
The proteins targeted for chloroplasts contain transit peptide sequence called stromal import
sequence or a stromal and thylakoid targeting sequence.
Import receptors and translocation complexes aid in targeting the protein to its respective
location. The endoproteases in stroma remove transit peptide sequences and the proteins fold into
functional form.
Proteins of the outer membrane complex are called Tocs
Inner membrane translocon complex proteins are called Tics
Proteins destined for thylakoid membrane will have both stromal and thylakoid targeting
sequence. cpSRP pathway is used for the insertion of these integral membrane proteins into the
thylakoid membrane..
Peroxisomes, mitochondria, and chloroplasts import proteins post-translationally using targeting signals. Peroxisomes import matrix and membrane proteins using peroxisome targeting signals and can import folded proteins through an unknown mechanism. Mitochondria import outer membrane, inner membrane, intermembrane, and matrix proteins using N-terminal signals and translocation complexes. Chloroplasts similarly import six compartment proteins using N-terminal transit peptides and translocation complexes. Both mitochondria and chloroplasts require proteins to be unfolded during import.
Mechanism of Targeting Protein and Signals Recognition Particle in Eukaryotic...Khalid Mukhtar
Mobile mammals can also have different protein isoforms and different protein molecules for men or women maximum proteins are encoded across the means of the nuclear genome and are synthesized within the cytoplasm side Proteins are within the ER side mitochondria chloroplast golgi peroxisomes nucleus , within the cytosol and within the membranes of those organelles, one sweet spot for diverse proteins requires a sophisticated labeling and sorting apparatus, we show how ribosomes attach to intracellular membranes, and to understand further that the major terminus of the nascent polypeptide chain includes peptide epitopes ،this arises from the ribosome and is determined by a nucleoprotein particle referred to as the signaling particle (SRP).
The document discusses extracellular vesicles (EVs) and their role in non-alcoholic steatohepatitis (NASH). It states that EVs originate from different cellular processes and can transfer cargo such as proteins and RNA between cells. Studies have shown that EVs isolated from mice with diet-induced NASH cause liver inflammation when transferred to healthy mice. EVs released from hepatocytes in response to toxic lipids are heterogeneous and regulated by kinases. They influence chemokine levels and immune cell recruitment to the liver.
Dynein and kinesin are motor proteins that play essential roles in chromosome dynamics by facilitating the intracellular transport of chromosomes along microtubules. Dynein moves chromosomes toward the nucleus by binding to adaptor proteins and walking toward the minus end of microtubules. Kinesin moves chromosomes away from the nucleus by binding to adaptor proteins and walking toward the plus end. Adaptor proteins link the motor proteins to chromosomes. Dynein and kinesin attachment allows precise control over chromosome positioning during processes like cell division and DNA repair.
The document provides an outline and overview of bacterial anatomy, physiology, growth, nutrition, metabolism, toxins, and bacteriocins. It discusses the structure and function of various bacterial cell organelles such as the cell wall, cytoplasmic membrane, mesosomes, nucleoid, plasmids, ribosomes, and inclusion bodies. It provides details on the cell wall structure of both gram-positive and gram-negative bacteria and describes various mechanisms of molecule movement through the cytoplasmic membrane, including passive diffusion, facilitated diffusion, group translocation, and active transport.
The document provides an outline and overview of bacterial anatomy, physiology, growth, nutrition, metabolism, toxins, and bacteriocins. It discusses the structure and function of various bacterial cell organelles such as the cell wall, cytoplasmic membrane, mesosomes, nucleoid, plasmids, ribosomes, and inclusion bodies. It provides details on the cell wall structure of both gram-positive and gram-negative bacteria and describes mechanisms of molecule movement through the cytoplasmic membrane.
This document provides an overview of bacterial anatomy, physiology, growth, nutrition, metabolism, toxins, and bacteriocins. It describes the structure and functions of bacterial cell organelles such as the cell wall, plasma membrane, mesosomes, nucleoid, plasmids, ribosomes, inclusion bodies, and endospores. It compares the cell walls of gram-positive and gram-negative bacteria and discusses bacterial movement of molecules, metabolism, and sporulation. The document is an educational reference on basic microbiology.
This document provides an overview of proteomics and protein-protein interactions. It begins with an introduction to proteomics, including its history and importance. It then discusses protein structure, including the primary, secondary, tertiary, and quaternary levels. The document outlines different types of proteomics, such as expression, structural, and functional proteomics. It also describes the various steps involved in proteome analysis, including sample preparation, separation, identification, and use of databases. The document discusses techniques for studying protein-protein interactions and provides examples like co-immunoprecipitation and yeast two-hybrid screening. Overall, the document provides a comprehensive overview of the key concepts and methods in the field of proteomics.
Membrane proteins play important roles in various cellular processes, such as cell adhesion, immune response, metabolism and signal transduction. They are popular targets for proteomics research and the common candidates for drug development. Shotgun proteomics methods are available for the identification of membrane proteins.
This document provides an overview of bacterial anatomy, physiology, growth, nutrition, metabolism, toxins, and bacteriocins. It begins with an outline of the topics to be covered, including the structure and function of bacterial cell organelles, growth and nutrition, metabolism, toxins, and bacteriocins. The document then discusses the structure of the bacterial cell and its various components such as the cell wall, plasma membrane, mesosomes, nucleoid, plasmids, ribosomes, inclusion bodies, and endospores. It provides details on the cell wall structure of gram-positive and gram-negative bacteria. The document also covers bacterial metabolism, toxins, and bacteriocins.
The document summarizes the wildlife diversity of the state of Odisha, India. It notes that Odisha has a large geographic area and forest cover, within which over 27 amphibian, 131 reptile, 524 bird, and 27 mammal species have been recorded, including many threatened species. Some of the important wildlife found in Odisha includes elephants, tigers, leopards, and various deer, squirrel, and bird species. The state has numerous wildlife sanctuaries, national parks, tiger and elephant reserves, and zoos established to support both in-situ and ex-situ conservation of Odisha's wildlife diversity.
Studies on mRNA surveillance and its role in alternative splicing.pptxSantosh Kumar Sahoo
This document outlines a Ph.D. research proposal on studying mRNA surveillance and its role in alternative splicing. The presentation includes background on mRNA surveillance mechanisms like nonsense-mediated decay (NMD), a review of literature on gaps in understanding NMD and its relationship to alternative splicing, objectives to study NMD factors and their role in degrading defective transcripts and interacting with alternative splicing, and proposed methodologies like protein purification and analysis. The expected outcomes are to better understand the mechanistic role of NMD in zebrafish and how it regulates alternative splice variants across eukaryotes.
The document discusses the structure of DNA as proposed by Watson and Crick in 1953. Some key points:
- Watson and Crick discovered that DNA has a double helix structure with two polynucleotide strands coiled around each other.
- The strands are anti-parallel, with nitrogenous bases projecting inward and forming hydrogen bonds between complementary base pairs of A-T and C-G.
- Their model explained how DNA replicates - the two strands separate and each acts as a template for a new partner strand, ensuring the base pairings are preserved.
This document discusses a thesis submitted to Centurion University of Technology and
Management to fulfill the requirements for a Master of Science degree in Zoology. The thesis,
titled "Understanding the involvement of N-terminal domain of FATs in interaction with
tumorogenic proteins," focuses on the structural and functional aspects of domains and motifs in
FAT family proteins (FAT1, FAT2, FAT3, and FAT4). Global bioinformatics databases were
used to identify putative protein interaction partners of the FAT proteins. Mutational analysis and
protein docking studies were then performed to analyze the interaction between domains of FAT
proteins and their interaction partners, providing insights into how FAT proteins maintain
cellular homeostasis and activate signaling
UNDERSTANDING THE INVOLVEMENT OF N-TERMINAL DOMAIN OF FATS IN INTERACTION WIT...Santosh Kumar Sahoo
Fat family members (FAT1, FAT2, FAT3, and FAT4) are human homologs of Drosophila Fat and are implicated in tumour suppression and planar cell polarity. Cellular homeostasis is largely maintained at the cellular level via transcription regulation, which can vary in response to physiological alterations. FAT atypical cadherin 1 (FAT1), which encodes a protocadherin, is one of the most frequently mutated genes in human cancer. FAT1 is thought to play a vital role in the maintenance of organ and cellular homeostasis, as well as activating a number of signalling pathways via protein-protein interactions, such as the Wnt/catenin, Hippo, and MAPK/ERK signaling pathways. Unregulated FAT1 expression can cause cancer and have a negative impact on prognosis. In this study, we focused on the structural and functional aspects of various domains and motifs of FAT1. Global bioinformatic databases resulted in streamlining a list of putative protein associates of FAT1. Since FAT1-mediated structural and functional alterations, as well as variations in FAT1 expression, contribute to disturbances in cellular homeostasis and result in patho-physiological disorders including cancer, we essentially focused on cancer-related genes functionally related to the FAT1. FAT1 is a huge protein composed of 4588 amino acid residues. By mutational analysis and further protein-protein docking studies using multiple bioinformatic tools it was confirmed that the C-terminus 4204-4214 and 4300-4400 amino acid residues are critical for interaction with cancer-related genes including Tumor necrosis factor, Myc proto-oncogene and Rela proto-oncogene. Interestingly, it was found that the small peptides corresponding to the C-terminus domain 4204-4214 and 4300-4400 of FAT1 effectively interact with tumor-suppressor genes. These evidences widens up the possibility of administering potential peptides when the FAT1 expression is inhibited. Our preliminary results will pave way forward in improving the prognosis and treatment of patients with cancer.
This document discusses air pollution sources and effects. It identifies four main types of air pollution sources: natural sources, stationary point sources, mobile sources, and waste disposal. Air pollutants are categorized based on their source, method of origin, chemical compound, and state of matter. Major air pollutants and their health and environmental effects are described. Methods for controlling air pollution are outlined, including using cleaner fuels and promoting public transportation. Summaries of the main sources of air pollution in India and its action plan for combating air pollution are also provided.
Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE)Santosh Kumar Sahoo
Two Dimensional Polyacrylamide gel Electrophoresis (2D-PAGE) is a technique used to separate and identify proteins in a biological sample. It involves two sequential steps - isoelectric focusing and SDS-PAGE - to separate proteins based on their isoelectric point and molecular weight. This allows visualization of up to 1,000s of individual protein spots on the gel. The protein spots can then be analyzed through techniques like mass spectrometry to identify specific proteins. While 2D-PAGE provides high resolution of complex protein mixtures, it has limitations such as a narrow dynamic range and difficulties separating some classes of proteins.
Pond construction as a challenge for fish processing industrySantosh Kumar Sahoo
The document discusses the importance of efficient pond construction for the fish processing industry, as productive ponds will provide the raw materials. It outlines the various steps involved in pond construction, including site preparation, dyke construction, inlet and outlet installation, and covering dykes with soil and vegetation. Efficient pond design and proper construction methods are necessary to maximize fish productivity and support the downstream fish processing industry.
Feed management in aquaculture involves choosing the right feed, using proper feeding methods, and ensuring cost effectiveness. The correct type of feed depends on the fish species, whether they are herbivores, carnivores, or omnivores. Feeds must provide proteins, carbohydrates, fats, vitamins, and minerals. Feeding should be frequent but in small quantities to avoid waste and pollution, using methods like automatic feeders. Record keeping helps control costs and monitor fish health.
1) Mud crabs undergo a complex life cycle beginning as larvae called zoea, which go through five zoeal stages and one megalopal stage before metamorphosing into juvenile crabs.
2) As juveniles, they migrate to estuaries where they mature over 18-24 months. Mature males and females mate, after which the females migrate offshore to spawn millions of eggs.
3) The eggs hatch into zoea larvae, restarting the cycle, with spawning occurring year-round in the tropics and during late spring to mid-autumn in subtropical and warm temperate areas.
Polymerase Chain Reaction
History of PCR
Instrumentation of PCR
Principle of PCR
Components of PCR
Steps of PCR
Optimal PCR Factors
Applications of PCR
Introduction
Fish Health Management GOALS
Principles of fish health management
Factors affecting fish health
Common symptoms of diseases
General preventive measures
Proper Health Management through manipulating the disease triangle
Conclusion
References
NCBI; Introduction, Homepage and about
Tools and database of NCBI
BLAST; Introduction, Homepage and types of BLAST
Some databases of NCBI
References
Acknowledgements
Fatty acid oxidation
Types of fatty acid oxidation
Overview of fatty acid oxidation
Beta-Oxidation of fatty acid
Steps in Beta-Oxidation of fatty acid
Stoichiometry of Beta oxidation
Reference
The document discusses the National Center for Biotechnology Information (NCBI). It provides background that NCBI is part of the National Library of Medicine and houses databases relevant to biotechnology and biomedicine. It describes some of NCBI's major databases, including GenBank for DNA sequences and PubMed for biomedical literature. The document also discusses the BLAST tool and provides examples of some of NCBI's databases, such as the Nucleotide, Protein, and Structural databases.
vector born diseases
malaria facts
Malaria; One of the world’s deadliest vectorborne diseases
Global malaria scenario; As for World
Malaria report 2020
Current Malaria scenario in INDIA
malaria vector control
prevention
Introduction
Fish Health Management GOALS
Principles of fish health management
Factors affecting fish health
Common symptoms of diseases
General preventive measures
Proper Health Management through Manipulating the disease triangle
Conclusion
References
This document summarizes fatty acid oxidation and beta-oxidation. It describes that fatty acid oxidation occurs in the mitochondria to break down fatty acids into acetyl-CoA, generating energy. Beta-oxidation involves four steps - oxidation, hydration, oxidation again, and cleavage - to sequentially remove two-carbon acetyl-CoA units from the fatty acid. The acetyl-CoA can then enter the citric acid cycle to generate more energy through oxidative phosphorylation.
Plants reproduce through fruit and seeds. Fruit contain seeds which, when mature, can be dispersed and grow into new plants. Seeds are the next generation of the parent plant that were formed within the fruit.
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
How to Make a Field Mandatory in Odoo 17Celine George
In Odoo, making a field required can be done through both Python code and XML views. When you set the required attribute to True in Python code, it makes the field required across all views where it's used. Conversely, when you set the required attribute in XML views, it makes the field required only in the context of that particular view.
This document provides an overview of wound healing, its functions, stages, mechanisms, factors affecting it, and complications.
A wound is a break in the integrity of the skin or tissues, which may be associated with disruption of the structure and function.
Healing is the body’s response to injury in an attempt to restore normal structure and functions.
Healing can occur in two ways: Regeneration and Repair
There are 4 phases of wound healing: hemostasis, inflammation, proliferation, and remodeling. This document also describes the mechanism of wound healing. Factors that affect healing include infection, uncontrolled diabetes, poor nutrition, age, anemia, the presence of foreign bodies, etc.
Complications of wound healing like infection, hyperpigmentation of scar, contractures, and keloid formation.
Exploiting Artificial Intelligence for Empowering Researchers and Faculty, In...Dr. Vinod Kumar Kanvaria
Exploiting Artificial Intelligence for Empowering Researchers and Faculty,
International FDP on Fundamentals of Research in Social Sciences
at Integral University, Lucknow, 06.06.2024
By Dr. Vinod Kumar Kanvaria
This slide is special for master students (MIBS & MIFB) in UUM. Also useful for readers who are interested in the topic of contemporary Islamic banking.
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Walmart Business+ and Spark Good for Nonprofits.pdfTechSoup
"Learn about all the ways Walmart supports nonprofit organizations.
You will hear from Liz Willett, the Head of Nonprofits, and hear about what Walmart is doing to help nonprofits, including Walmart Business and Spark Good. Walmart Business+ is a new offer for nonprofits that offers discounts and also streamlines nonprofits order and expense tracking, saving time and money.
The webinar may also give some examples on how nonprofits can best leverage Walmart Business+.
The event will cover the following::
Walmart Business + (https://business.walmart.com/plus) is a new shopping experience for nonprofits, schools, and local business customers that connects an exclusive online shopping experience to stores. Benefits include free delivery and shipping, a 'Spend Analytics” feature, special discounts, deals and tax-exempt shopping.
Special TechSoup offer for a free 180 days membership, and up to $150 in discounts on eligible orders.
Spark Good (walmart.com/sparkgood) is a charitable platform that enables nonprofits to receive donations directly from customers and associates.
Answers about how you can do more with Walmart!"
Chapter wise All Notes of First year Basic Civil Engineering.pptxDenish Jangid
Chapter wise All Notes of First year Basic Civil Engineering
Syllabus
Chapter-1
Introduction to objective, scope and outcome the subject
Chapter 2
Introduction: Scope and Specialization of Civil Engineering, Role of civil Engineer in Society, Impact of infrastructural development on economy of country.
Chapter 3
Surveying: Object Principles & Types of Surveying; Site Plans, Plans & Maps; Scales & Unit of different Measurements.
Linear Measurements: Instruments used. Linear Measurement by Tape, Ranging out Survey Lines and overcoming Obstructions; Measurements on sloping ground; Tape corrections, conventional symbols. Angular Measurements: Instruments used; Introduction to Compass Surveying, Bearings and Longitude & Latitude of a Line, Introduction to total station.
Levelling: Instrument used Object of levelling, Methods of levelling in brief, and Contour maps.
Chapter 4
Buildings: Selection of site for Buildings, Layout of Building Plan, Types of buildings, Plinth area, carpet area, floor space index, Introduction to building byelaws, concept of sun light & ventilation. Components of Buildings & their functions, Basic concept of R.C.C., Introduction to types of foundation
Chapter 5
Transportation: Introduction to Transportation Engineering; Traffic and Road Safety: Types and Characteristics of Various Modes of Transportation; Various Road Traffic Signs, Causes of Accidents and Road Safety Measures.
Chapter 6
Environmental Engineering: Environmental Pollution, Environmental Acts and Regulations, Functional Concepts of Ecology, Basics of Species, Biodiversity, Ecosystem, Hydrological Cycle; Chemical Cycles: Carbon, Nitrogen & Phosphorus; Energy Flow in Ecosystems.
Water Pollution: Water Quality standards, Introduction to Treatment & Disposal of Waste Water. Reuse and Saving of Water, Rain Water Harvesting. Solid Waste Management: Classification of Solid Waste, Collection, Transportation and Disposal of Solid. Recycling of Solid Waste: Energy Recovery, Sanitary Landfill, On-Site Sanitation. Air & Noise Pollution: Primary and Secondary air pollutants, Harmful effects of Air Pollution, Control of Air Pollution. . Noise Pollution Harmful Effects of noise pollution, control of noise pollution, Global warming & Climate Change, Ozone depletion, Greenhouse effect
Text Books:
1. Palancharmy, Basic Civil Engineering, McGraw Hill publishers.
2. Satheesh Gopi, Basic Civil Engineering, Pearson Publishers.
3. Ketki Rangwala Dalal, Essentials of Civil Engineering, Charotar Publishing House.
4. BCP, Surveying volume 1
Chapter wise All Notes of First year Basic Civil Engineering.pptx
Mitochondrial protein targeting
1. Name - Ipsita Sahoo
Reg no- 200705180160
Guided by- Mr. Gagan Kumar Panigrahi
School of Applied Science, CUTM, BBSR
M Sc. 1st year Zoology
Subject- Cell and Molecular Biology
Topic- “Mitochondrial Protein Targeting”
Session- 2020-22
2. Introduction
Overview of Protein targeting
Protein Import Into Mitochondrial Matrix
Protein transport from cytosol to inner mitochondrial
membrane
Protein transport from cytosol to mitochondrial
inter-membrane space
Conclusion
Reference
CONTENTS
3. Introduction
Protein targeting or protein sorting is a biological mechanism by
which proteins are transported to their appropriate destinations i.e.
within or outside the cell.
Since the translation of mRNA into protein by a ribosome takes place
within the cytosol, proteins destined for secretion or a
specific organelle must be translocated. This process can occur during
translation, known as co-translational translocation, or after translation
is complete, known as post-translational translocation.
5. Protein targeting to Mitochondria
Mitochondrial proteins are synthesized by 80S cytosolic as well as
70S matrix ribosome.
About 99% of mitochondrial proteins are encoded by nuclear gene
and are synthesized as precursors on cytosolic-ribosomes.
Proteins synthesized by cytosolic-ribosomes are translocated into
mitochondria post-translationally.
Inter
membra
ne space
6. Requirement of Mitochondrial protein
import
Mitochondrial protein import requires translocation complexes that
mediate translocation and mitochondrial targeting signal (MTS)
sequences.
a) Translocation Complexes
Two distinct translocation complex are situated in outer and
inner mitochondrial membranes referred to as TOM (Translocase
of the outer membrane) complex and TIM (Translocase of the
inner membrane) complex.
b) Mitochondrial Targeting Signal
• Length about 10-30 amino acid residues.
• Rich in +ve charged basic amino acid
(Arginine and lysine)
N-terminal cleavable
matrix targeting
sequences (Presequences)
• These proteins includes all outer membrane
protein.
Non cleavable internal
targeting sequences
7. Protein Import Into Mitochondrial Matrix
Most of matrix targeting proteins enter into mt matrix contain N-
terminal cleavable targeting sequences & synthesized by cytosolic 80S.
10. Proteins sorted to mitochondrial destinations other than the matrix
usually contain two or more targeting sequences, one of which may
be an N-terminal matrix-targeting Sequence.
Some mitochondrial proteins destined for the inter-membrane
space or inner membrane are first imported into the matrix and then
redirected; others never enter the matrix but go directly to their final
location.
Conclusion
11. Reference
Nelson DL (January 2017). Lehninger principles of biochemistry.
Cox, Michael M.,, Lehninger, Albert L. (Seventh ed.). New York,
NY. ISBN 978-1-4641-2611-6. OCLC 986827885.
Sommer MS, Schleiff E (August 2014). "Protein targeting and
transport as a necessary consequence of increased cellular
complexity". Cold Spring Harbor Perspectives in Biology. 6 (8):
a016055. doi:10.1101/cshperspect.a016055. PMC 4107987. PMID 250
85907.
Walter P, Ibrahimi I, Blobel G (November 1981). "Translocation of
proteins across the endoplasmic reticulum. I. Signal recognition
protein (SRP) binds to in-vitro-assembled polysomes synthesizing
secretory protein". The Journal of Cell Biology. 91 (2 Pt 1): 545–
50. doi:10.1083/jcb.91.2.545. PMC 2111968. PMID 7309795.
Lodish H, Berk A, Kaiser C, Krieger M, Bretscher A, Ploegh H,
Amon A, Martin K (2008). Molecular Cell Biology (8th ed.). New
York: W.H. Freeman and Company. pp. 591–592. ISBN 978-1-4641-
8339-3.