Post transcriptional modifications
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Translational Regulation of Development
The document discusses various mechanisms of translational regulation of gene expression, including:
1. Differential mRNA longevity, selective inhibition of mRNA translation in stored oocyte mRNAs, microRNAs, and control of RNA expression through cytoplasmic localization.
2. MicroRNAs inhibit translation by packaging with proteins to form RNA-induced silencing complexes that bind to target RNA.
3. mRNAs can be localized to specific cell regions through diffusion and anchoring, localized protection, or active transport along the cytoskeleton.
Post trans mod-and_protein sorting
Post-translational modifications (PTMs) are key mechanisms that increase proteomic diversity and regulate cellular activity. PTMs such as phosphorylation, methylation, acetylation, and ubiquitination occur through the addition of functional groups to specific amino acids on a protein by enzymes. These modifications can regulate protein activity, stability, localization, and degradation. Proteins are targeted to different intracellular compartments through sorting signals and transport mechanisms like gated transport, transmembrane transport, and vesicular transport.
Posttranslationmodification new new new new
Posttranslational modification (PTM) is a key step in protein biosynthesis. After proteins are synthesized by ribosomes translating mRNA into polypeptide chains, the chains undergo PTM such as folding, cutting, and other processes to become mature proteins. PTMs extend the range of protein functions by attaching biochemical groups like phosphates or making structural changes like formation of disulfide bridges.
Co and post translationational modification of proteins
This document discusses co-translational and post-translational modifications of proteins. It begins with an introduction to protein modification and defines co-translational and post-translational modifications. It then covers various co-translational modifications including regulation of translation, protein folding, and enzymes that catalyze protein folding. Post-translational modifications discussed include protein cleavage, glycosylation, addition of GPI anchors, ubiquitination, and phosphorylation. The document provides examples and details for many of the modification processes.
JSHS_Paper_BK_Final_Draft_Brian_Kam (6)
1) The author investigated how phosphorylation regulates the kinesin-13 protein KLP10A in Drosophila S2 cells.
2) Immunofluorescence imaging showed that endogenous KLP10A localizes to microtubule ends in interphase cells. Depleting KLP10A altered microtubule morphology.
3) Live cell imaging of S2 cells expressing mRFP-tagged KLP10A or a phosphomimetic S573E mutant found that phosphorylation affects KLP10A's intracellular localization and interaction with microtubules.
Translation and Post Translational Modification
This document discusses the process of translation. It begins by defining translation as the biosynthesis of a protein inside a living cell using the genetic code. It then describes the three main steps of translation - initiation, elongation, and termination. Initiation involves assembling the ribosome complex on prokaryotes and eukaryotes. Elongation is the process of amino acid chain elongation through tRNA and elongation factors. Termination occurs when a stop codon is reached, signaling the release of the polypeptide chain. The document also briefly mentions post-translational modifications that can occur after translation is complete.
Protein sorting and targeting
protein sorting and targeting ,
protein generation and their distribution to various organelles and out of the cell.
Post translational modifications
a very brief and informative presentation on PTM......... presented in CEMB by Saadia Aslam, Punjab University Lahore.
Recommended
Translational Regulation of Development
The document discusses various mechanisms of translational regulation of gene expression, including:
1. Differential mRNA longevity, selective inhibition of mRNA translation in stored oocyte mRNAs, microRNAs, and control of RNA expression through cytoplasmic localization.
2. MicroRNAs inhibit translation by packaging with proteins to form RNA-induced silencing complexes that bind to target RNA.
3. mRNAs can be localized to specific cell regions through diffusion and anchoring, localized protection, or active transport along the cytoskeleton.
Post trans mod-and_protein sorting
Post-translational modifications (PTMs) are key mechanisms that increase proteomic diversity and regulate cellular activity. PTMs such as phosphorylation, methylation, acetylation, and ubiquitination occur through the addition of functional groups to specific amino acids on a protein by enzymes. These modifications can regulate protein activity, stability, localization, and degradation. Proteins are targeted to different intracellular compartments through sorting signals and transport mechanisms like gated transport, transmembrane transport, and vesicular transport.
Posttranslationmodification new new new new
Posttranslational modification (PTM) is a key step in protein biosynthesis. After proteins are synthesized by ribosomes translating mRNA into polypeptide chains, the chains undergo PTM such as folding, cutting, and other processes to become mature proteins. PTMs extend the range of protein functions by attaching biochemical groups like phosphates or making structural changes like formation of disulfide bridges.
Co and post translationational modification of proteins
This document discusses co-translational and post-translational modifications of proteins. It begins with an introduction to protein modification and defines co-translational and post-translational modifications. It then covers various co-translational modifications including regulation of translation, protein folding, and enzymes that catalyze protein folding. Post-translational modifications discussed include protein cleavage, glycosylation, addition of GPI anchors, ubiquitination, and phosphorylation. The document provides examples and details for many of the modification processes.
JSHS_Paper_BK_Final_Draft_Brian_Kam (6)
1) The author investigated how phosphorylation regulates the kinesin-13 protein KLP10A in Drosophila S2 cells.
2) Immunofluorescence imaging showed that endogenous KLP10A localizes to microtubule ends in interphase cells. Depleting KLP10A altered microtubule morphology.
3) Live cell imaging of S2 cells expressing mRFP-tagged KLP10A or a phosphomimetic S573E mutant found that phosphorylation affects KLP10A's intracellular localization and interaction with microtubules.
Translation and Post Translational Modification
This document discusses the process of translation. It begins by defining translation as the biosynthesis of a protein inside a living cell using the genetic code. It then describes the three main steps of translation - initiation, elongation, and termination. Initiation involves assembling the ribosome complex on prokaryotes and eukaryotes. Elongation is the process of amino acid chain elongation through tRNA and elongation factors. Termination occurs when a stop codon is reached, signaling the release of the polypeptide chain. The document also briefly mentions post-translational modifications that can occur after translation is complete.
Protein sorting and targeting
protein sorting and targeting ,
protein generation and their distribution to various organelles and out of the cell.
Post translational modifications
a very brief and informative presentation on PTM......... presented in CEMB by Saadia Aslam, Punjab University Lahore.
Biosynthesis of protein in eukariotes
INTRODUCTION
HISTORY
MECHANISM OF PROTEIN SYNTHESIS
TRANSCRIPTION
TRANSLATION
TRANSCRIPTION
INITIATION
ELONGATION
TERMINATION
TRANSLATION
AMINOACYLATION OF tRNA
INITIATION OF POLYPEPTIDE CHAIN
ELONGATION
TERMINATION
CONCLUSION
REFERENCES
Protein targetting
Protein sorting and targeting involves transporting proteins to the appropriate locations within or outside the cell. There are several pathways for protein targeting, including vesicular transport between organelles like the ER and Golgi, as well as transport of proteins into organelles like mitochondria and peroxisomes. Targeting signals like presequences and internal targeting peptides direct cellular transport machinery to correctly position proteins. Lipidation is another method to target proteins to specific membranes through modifications like glycosyl phosphatidylinositol anchors or myristoylation.
Post-Translational Modification
Post-translational modifications are important biochemical mechanisms that regulate protein function. Common types of post-translational modifications include phosphorylation, hydroxylation, glycosylation, and methylation. These modifications occur on amino acid side chains or termini and are catalyzed by specific enzymes. For example, phosphorylation regulates enzyme activity, while hydroxylation and glycosylation of amino acids are required for collagen assembly and function. Overall, post-translational modifications expand the functional diversity of the proteome.
Galactose operon slide share
The gal operon is a prokaryotic operon, which encodes enzymes necessary for galactose metabolism. The operon contains two operators, OE and OI. The former is just before the promoter, and the latter is just after the galE gene.This slide share includes some of the reasearch done on the galactose operons explained with review articles
Gerstner et al PLoS One 2008
This document reports that brain fatty acid binding protein (Fabp7) mRNA levels in the brain undergo diurnal changes in adult rodents. Specifically:
1) Fabp7 mRNA levels were higher during the light period and lower during the dark period in brain regions involved in sleep and activity like the tuberomammillary nucleus, pons, and locus coeruleus.
2) This diurnal pattern of Fabp7 mRNA expression occurred throughout the entire brain and was also seen in granule cell precursors of the adult hippocampus.
3) In contrast, the fatty acid binding protein Fabp5 did not show diurnal changes in these brain regions, indicating Fabp7 expression has a unique synchronized
Protein targeting
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.
Cognitive neuroscience active zone
1) The active zone is composed of an evolutionarily conserved protein complex containing RIM, Munc13, RIM-BP, α-liprin, and ELKS proteins as core constituents. This complex docks and primes synaptic vesicles for exocytosis.
2) In addition to transmitting information, synapses transform information encoded in bursts of action potentials through short-term and long-term plasticity mediated by the active zone protein complex.
3) The five core proteins work together to recruit voltage-gated calcium channels to the active zone, position the active zone opposite postsynaptic specializations, and mediate both short-term and long-term presynaptic plasticity.
Protein targetting ppt (1)
This document summarizes protein targeting mechanisms in cells. It discusses how signal sequences direct proteins to different organelles like the endoplasmic reticulum, mitochondria, chloroplasts and nucleus. The signal sequence is cleaved after the protein reaches its destination. Glycosylation in the ER plays a key role in targeting lysosomal enzymes. Mitochondrial and chloroplast proteins use a different targeting mechanism after full synthesis. Receptor-mediated endocytosis imports some extracellular proteins by binding to receptors and forming clathrin-coated vesicles.
Protein targeting or translocation of proteins
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.
Protein targeting ajay
Protein targeting is the process by which proteins are directed to specific locations after synthesis. Signal sequences on proteins guide their transport, as discovered by Gunter Blobel who won the Nobel Prize for this work. Protein targeting is important because proteins must be sorted to the correct locations, like organelles, to properly function. Eukaryotic protein targeting is complex due to many intracellular compartments and can involve posttranslational modifications and receptor-mediated transport mechanisms. Correct protein sorting is vital for cell function and errors can cause disease.
Transcription
Transcription is the process of copying genetic information from DNA to RNA. It involves three main stages - initiation, elongation, and termination. RNA polymerase binds to promoter sequences near genes and uses the DNA as a template to synthesize complementary RNA strands. In eukaryotes, the primary RNA transcripts undergo further processing including splicing, capping, and polyadenylation. Transcription and its regulation allow genetic information to be selectively expressed as needed and provide an additional layer of gene control.
Protein Localization
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.
Gene regulation in prokaryotes
The document discusses gene regulation in prokaryotes. It introduces the concept of operons, which are clusters of genes under the control of a single promoter. The lac operon in E. coli is described in detail. The lac operon contains three structural genes that encode proteins involved in lactose metabolism. In the absence of lactose, a repressor protein binds to the operator region and blocks transcription. However, in the presence of lactose, the lactose binds to the repressor and changes its shape so it cannot bind to the operator, allowing transcription and expression of the structural genes.
RNA Processing in Devlopmental biology
The document discusses RNA processing during cellular differentiation. It provides an overview of gene expression, noting that different cell types contain the same DNA but produce different proteins. RNA processing in eukaryotes involves RNA selection and splicing. RNA splicing allows different combinations of exons to form different proteins. The document uses examples of sex determination in Drosophila and alternative splicing of the tropomyosin gene to produce different protein isoforms in various tissues.
Gene regulation
The document summarizes regulation of gene expression in prokaryotes and eukaryotes. In prokaryotes, genes are organized into operons containing a promoter, operator, and multiple coding sequences. The lac operon in E.coli contains genes regulated by the repressor protein LacI and induced by lactose. In eukaryotes, gene expression is regulated at multiple levels including transcription, RNA processing, transport, translation and degradation. Mechanisms include histone modification, DNA methylation, hormone signaling, polyadenylation, splicing, transport and protein degradation.
Lec9_Organelle Targeting
Proteins destined for chloroplasts and mitochondria are synthesized with targeting signals that direct them to the appropriate organelle. Chloroplast proteins have an N-terminal transit peptide that guides them through chloroplast membranes. There are several pathways for transporting chloroplast proteins across the thylakoid membrane to the lumen. Mitochondria import uses a different membrane machinery than chloroplasts, and requires an electrochemical potential across the inner membrane. Some proteins are dually targeted to both organelles.
PIIS2211124716313158
1) Loss of the kinase NEK1 in mice leads to abnormal retention of the cohesin component SMC3 on chromosome arms during meiotic prophase I.
2) Mass spectrometry analysis found that WAPL, a protein involved in cohesin removal, has abnormal elevated phosphorylation at a specific residue in NEK1-deficient mice.
3) This suggests NEK1 may regulate WAPL and cohesin removal during meiosis, though not directly as its loss leads to increased rather than decreased WAPL phosphorylation. NEK1 likely acts through another protein to phosphorylate or dephosphorylate WAPL.
PROTEIN TARGETING
1. Proteins in eukaryotic cells are synthesized in the cytosol but must be targeted to various intracellular destinations like organelles. They use signal sequences and membrane receptors to direct their transport.
2. In the ER, proteins are modified through glycosylation and folding before being sent to the Golgi apparatus for further processing and sorting to their final locations like the plasma membrane or lysosomes.
3. Mitochondria and chloroplasts import proteins using signal sequences after full synthesis, while nuclear transport relies on non-cleaved NLS sequences and importin proteins.
4. Bacteria also use cleaved signal sequences and chaperones to transport proteins through membrane complexes. Cells import proteins through receptor-mediated
Post Translational Modification
Post-translational modifications are chemical changes made to proteins after translation. Some key post-translational modifications include phosphorylation, glycosylation, ubiquitination, and acetylation. Phosphorylation involves adding phosphate groups and is important for processes like cell signaling. Glycosylation attaches carbohydrate groups and affects protein structure and function. Ubiquitination labels proteins for destruction, regulating processes like the cell cycle. Acetylation adds acetyl groups and is involved in gene regulation. These post-translational modifications are important for regulating protein activity, localization, and interactions in the cell.
Post-Transcriptional Modification of Eukaryotic mRNA
Hello everyone, I am Dr. Ujwalkumar Trivedi, Head of Biotechnology Department at Marwadi University Rajkot. I teach Molecular Biology to the students of M.Sc. Microbiology and Biotechnology.
The current presentation describes various co-transcriptional and post-transcriptional RNA modifications in eukaryotic cells. The following processes are described in detail:
1. 5' mRNA Capping
2. Splicing
3. Alternative Splicing
4. 3' Polyadenylation
5. RNA Editing
Enjoy Reading.
RNA_splicing_ppt.ppt
This document provides an overview of post-transcriptional gene control mechanisms. It discusses processing of eukaryotic pre-mRNA including 5' capping, polyadenylation, and splicing. Splicing involves spliceosome complexes containing small nuclear RNAs. The document also covers regulation of alternative splicing and mechanisms of gene repression by microRNAs and short interfering RNAs.
13-miller-chap-8-lecture (1).ppt
This document provides an overview of post-transcriptional gene control mechanisms. It discusses processing of eukaryotic pre-mRNA including 5' capping, polyadenylation, and splicing. Splicing involves spliceosome complexes containing small nuclear RNAs. The document also covers regulation of alternative splicing and mechanisms of gene repression by microRNAs and short interfering RNAs.
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Biosynthesis of protein in eukariotes
INTRODUCTION
HISTORY
MECHANISM OF PROTEIN SYNTHESIS
TRANSCRIPTION
TRANSLATION
TRANSCRIPTION
INITIATION
ELONGATION
TERMINATION
TRANSLATION
AMINOACYLATION OF tRNA
INITIATION OF POLYPEPTIDE CHAIN
ELONGATION
TERMINATION
CONCLUSION
REFERENCES
Protein targetting
Protein sorting and targeting involves transporting proteins to the appropriate locations within or outside the cell. There are several pathways for protein targeting, including vesicular transport between organelles like the ER and Golgi, as well as transport of proteins into organelles like mitochondria and peroxisomes. Targeting signals like presequences and internal targeting peptides direct cellular transport machinery to correctly position proteins. Lipidation is another method to target proteins to specific membranes through modifications like glycosyl phosphatidylinositol anchors or myristoylation.
Post-Translational Modification
Post-translational modifications are important biochemical mechanisms that regulate protein function. Common types of post-translational modifications include phosphorylation, hydroxylation, glycosylation, and methylation. These modifications occur on amino acid side chains or termini and are catalyzed by specific enzymes. For example, phosphorylation regulates enzyme activity, while hydroxylation and glycosylation of amino acids are required for collagen assembly and function. Overall, post-translational modifications expand the functional diversity of the proteome.
Galactose operon slide share
The gal operon is a prokaryotic operon, which encodes enzymes necessary for galactose metabolism. The operon contains two operators, OE and OI. The former is just before the promoter, and the latter is just after the galE gene.This slide share includes some of the reasearch done on the galactose operons explained with review articles
Gerstner et al PLoS One 2008
This document reports that brain fatty acid binding protein (Fabp7) mRNA levels in the brain undergo diurnal changes in adult rodents. Specifically:
1) Fabp7 mRNA levels were higher during the light period and lower during the dark period in brain regions involved in sleep and activity like the tuberomammillary nucleus, pons, and locus coeruleus.
2) This diurnal pattern of Fabp7 mRNA expression occurred throughout the entire brain and was also seen in granule cell precursors of the adult hippocampus.
3) In contrast, the fatty acid binding protein Fabp5 did not show diurnal changes in these brain regions, indicating Fabp7 expression has a unique synchronized
Protein targeting
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.
Cognitive neuroscience active zone
1) The active zone is composed of an evolutionarily conserved protein complex containing RIM, Munc13, RIM-BP, α-liprin, and ELKS proteins as core constituents. This complex docks and primes synaptic vesicles for exocytosis.
2) In addition to transmitting information, synapses transform information encoded in bursts of action potentials through short-term and long-term plasticity mediated by the active zone protein complex.
3) The five core proteins work together to recruit voltage-gated calcium channels to the active zone, position the active zone opposite postsynaptic specializations, and mediate both short-term and long-term presynaptic plasticity.
Protein targetting ppt (1)
This document summarizes protein targeting mechanisms in cells. It discusses how signal sequences direct proteins to different organelles like the endoplasmic reticulum, mitochondria, chloroplasts and nucleus. The signal sequence is cleaved after the protein reaches its destination. Glycosylation in the ER plays a key role in targeting lysosomal enzymes. Mitochondrial and chloroplast proteins use a different targeting mechanism after full synthesis. Receptor-mediated endocytosis imports some extracellular proteins by binding to receptors and forming clathrin-coated vesicles.
Protein targeting or translocation of proteins
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.
Protein targeting ajay
Protein targeting is the process by which proteins are directed to specific locations after synthesis. Signal sequences on proteins guide their transport, as discovered by Gunter Blobel who won the Nobel Prize for this work. Protein targeting is important because proteins must be sorted to the correct locations, like organelles, to properly function. Eukaryotic protein targeting is complex due to many intracellular compartments and can involve posttranslational modifications and receptor-mediated transport mechanisms. Correct protein sorting is vital for cell function and errors can cause disease.
Transcription
Transcription is the process of copying genetic information from DNA to RNA. It involves three main stages - initiation, elongation, and termination. RNA polymerase binds to promoter sequences near genes and uses the DNA as a template to synthesize complementary RNA strands. In eukaryotes, the primary RNA transcripts undergo further processing including splicing, capping, and polyadenylation. Transcription and its regulation allow genetic information to be selectively expressed as needed and provide an additional layer of gene control.
Protein Localization
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.
Gene regulation in prokaryotes
The document discusses gene regulation in prokaryotes. It introduces the concept of operons, which are clusters of genes under the control of a single promoter. The lac operon in E. coli is described in detail. The lac operon contains three structural genes that encode proteins involved in lactose metabolism. In the absence of lactose, a repressor protein binds to the operator region and blocks transcription. However, in the presence of lactose, the lactose binds to the repressor and changes its shape so it cannot bind to the operator, allowing transcription and expression of the structural genes.
RNA Processing in Devlopmental biology
The document discusses RNA processing during cellular differentiation. It provides an overview of gene expression, noting that different cell types contain the same DNA but produce different proteins. RNA processing in eukaryotes involves RNA selection and splicing. RNA splicing allows different combinations of exons to form different proteins. The document uses examples of sex determination in Drosophila and alternative splicing of the tropomyosin gene to produce different protein isoforms in various tissues.
Gene regulation
The document summarizes regulation of gene expression in prokaryotes and eukaryotes. In prokaryotes, genes are organized into operons containing a promoter, operator, and multiple coding sequences. The lac operon in E.coli contains genes regulated by the repressor protein LacI and induced by lactose. In eukaryotes, gene expression is regulated at multiple levels including transcription, RNA processing, transport, translation and degradation. Mechanisms include histone modification, DNA methylation, hormone signaling, polyadenylation, splicing, transport and protein degradation.
Lec9_Organelle Targeting
Proteins destined for chloroplasts and mitochondria are synthesized with targeting signals that direct them to the appropriate organelle. Chloroplast proteins have an N-terminal transit peptide that guides them through chloroplast membranes. There are several pathways for transporting chloroplast proteins across the thylakoid membrane to the lumen. Mitochondria import uses a different membrane machinery than chloroplasts, and requires an electrochemical potential across the inner membrane. Some proteins are dually targeted to both organelles.
PIIS2211124716313158
1) Loss of the kinase NEK1 in mice leads to abnormal retention of the cohesin component SMC3 on chromosome arms during meiotic prophase I.
2) Mass spectrometry analysis found that WAPL, a protein involved in cohesin removal, has abnormal elevated phosphorylation at a specific residue in NEK1-deficient mice.
3) This suggests NEK1 may regulate WAPL and cohesin removal during meiosis, though not directly as its loss leads to increased rather than decreased WAPL phosphorylation. NEK1 likely acts through another protein to phosphorylate or dephosphorylate WAPL.
PROTEIN TARGETING
1. Proteins in eukaryotic cells are synthesized in the cytosol but must be targeted to various intracellular destinations like organelles. They use signal sequences and membrane receptors to direct their transport.
2. In the ER, proteins are modified through glycosylation and folding before being sent to the Golgi apparatus for further processing and sorting to their final locations like the plasma membrane or lysosomes.
3. Mitochondria and chloroplasts import proteins using signal sequences after full synthesis, while nuclear transport relies on non-cleaved NLS sequences and importin proteins.
4. Bacteria also use cleaved signal sequences and chaperones to transport proteins through membrane complexes. Cells import proteins through receptor-mediated
Post Translational Modification
Post-translational modifications are chemical changes made to proteins after translation. Some key post-translational modifications include phosphorylation, glycosylation, ubiquitination, and acetylation. Phosphorylation involves adding phosphate groups and is important for processes like cell signaling. Glycosylation attaches carbohydrate groups and affects protein structure and function. Ubiquitination labels proteins for destruction, regulating processes like the cell cycle. Acetylation adds acetyl groups and is involved in gene regulation. These post-translational modifications are important for regulating protein activity, localization, and interactions in the cell.
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Similar to Post transcriptional modifications
Post-Transcriptional Modification of Eukaryotic mRNA
Hello everyone, I am Dr. Ujwalkumar Trivedi, Head of Biotechnology Department at Marwadi University Rajkot. I teach Molecular Biology to the students of M.Sc. Microbiology and Biotechnology.
The current presentation describes various co-transcriptional and post-transcriptional RNA modifications in eukaryotic cells. The following processes are described in detail:
1. 5' mRNA Capping
2. Splicing
3. Alternative Splicing
4. 3' Polyadenylation
5. RNA Editing
Enjoy Reading.
RNA_splicing_ppt.ppt
This document provides an overview of post-transcriptional gene control mechanisms. It discusses processing of eukaryotic pre-mRNA including 5' capping, polyadenylation, and splicing. Splicing involves spliceosome complexes containing small nuclear RNAs. The document also covers regulation of alternative splicing and mechanisms of gene repression by microRNAs and short interfering RNAs.
13-miller-chap-8-lecture (1).ppt
This document provides an overview of post-transcriptional gene control mechanisms. It discusses processing of eukaryotic pre-mRNA including 5' capping, polyadenylation, and splicing. Splicing involves spliceosome complexes containing small nuclear RNAs. The document also covers regulation of alternative splicing and mechanisms of gene repression by microRNAs and short interfering RNAs.
Group 6 - Post Transcriptional Modifications (RNA Splicng and ALternative Spl...
Alternative splicing allows a single gene to encode multiple proteins. It occurs when introns are differentially spliced out of pre-mRNA, allowing exons to be joined in various combinations. This increases proteome diversity and regulates key cellular processes. Alternative splicing is regulated by elements in exons and introns that bind proteins to promote or suppress inclusion of sequence regions. Errors can contribute to diseases.
post transcriptional modifications
Three types of RNA molecules undergo post-transcriptional modification before becoming functional: mRNA, tRNA, and rRNA. These modifications include polyadenylation, 5' capping, and splicing. Polyadenylation adds around 80-250 adenine residues to the 3' end of mRNA to protect it from degradation. 5' capping adds a 7-methylguanosine residue to the 5' end of mRNA to also protect it from degradation and aid nuclear export and translation initiation. Splicing removes intron sequences from precursor mRNA by two transesterification reactions.
Post transcriptional modification
Detailed presentation on splicing, poly adenylation and capping of mRNA with diagrammatic description.
hn RNA processing
The document discusses various processes involved in eukaryotic mRNA processing. It explains that in eukaryotes, pre-mRNA undergoes 5' capping, 3' cleavage and polyadenylation, splicing, and methylation to become a mature mRNA. These processes are guided by hnRNP and snRNP particles. The document also discusses alternative mRNA processing mechanisms like alternative splicing and polyadenylation that generate multiple mRNA isoforms from a single pre-mRNA.
Lecture 3 Post Ts Modification-lecture notes.pdf
The document discusses post-transcriptional modifications that occur in eukaryotic mRNA. It describes three major modifications: 1) 5' capping, which adds a 7-methylguanosine cap to protect the mRNA and enhance translation, 2) 3' polyadenylation, which adds a poly-A tail to stabilize the mRNA and influence translation and stability, and 3) splicing, by which introns are removed from pre-mRNA through the spliceosome complex to produce mature mRNA for translation.
Post-Transcriptional Modification
The document summarizes several key post-transcriptional processes involved in modifying mRNA in eukaryotes. These include 5' capping, 3' polyadenylation, intron removal through splicing, and the role of heterogeneous ribonucleoproteins (hnRNP) in transporting mRNA out of the nucleus. The splicing process involves small nuclear RNAs binding in a spliceosome to catalyze two transesterification reactions that remove introns and ligate exons. Mature mRNA can also be generated through trans-splicing of separate RNA molecules or alternative splicing of different exons from the same gene. Nuclear pore complexes selectively transport molecules including mRNA in and out of the nucleus.
Structure and function of Messenger RNA (mRNA )
This presentation of 42 slides delivers information about structure,function synthesis , life span of both prokaryotic and eukaryotic messenger RNA also about role in protein sorting and targetting
RNA Splicing presentation.pptx
RNA splicing is a biological process where a newly synthesized pre-mRNA transcript is processed and transformed into mRNA. It involves the removing of non-coding regions of RNA (introns) and the joining of the coding regions (exons).
Post transcriptional modifications
Post-transcriptional modifications are a set of processes that alter RNA transcripts following transcription to produce mature functional RNAs. These include adding a 5' cap, polyadenylating the 3' end with a poly-A tail, and splicing out introns. The cap protects the RNA from degradation and aids in nuclear export and translation. Polyadenylation and splicing make the RNA more stable and translatable. Splicing involves snRNPs that recognize splice sites and catalyze intron removal through transesterification reactions. Alternative splicing allows single genes to encode multiple proteins.
mRNA This splicing
Split genes contain both coding (exon) and non-coding (intron) regions. During mRNA splicing, introns are removed from pre-mRNA and exons are joined together to form mature mRNA. This process is catalyzed by the spliceosome, a complex of five small nuclear RNAs and numerous proteins. The spliceosome facilitates two transesterification reactions which remove the intron and ligate the exons, allowing gene sequences to code for multiple proteins through alternative splicing. Splicing increases gene and protein diversity in the cell.
281 lec14 eukaryptic_transcription
The document summarizes transcription in eukaryotes. It discusses that eukaryotes have multiple RNA polymerases that transcribe different RNA molecules. It describes the structure of eukaryotic genes including exons, introns, the 5' UTR and 3' UTR. The transcription process involves RNA polymerase binding to promoters and assembling with transcription factors to form the preinitiation complex. The complex melts the promoter DNA and initiates transcription. The pre-mRNA undergoes 5' capping, 3' polyadenylation, and intron splicing to become a mature mRNA, unlike prokaryotes where transcription and translation are coupled.
RNA SPLICING
RNA splicing is a process where introns are removed from precursor messenger RNA (pre-mRNA) and exons are joined together to produce mature mRNA. It occurs in the nucleus and is essential for eukaryotes to produce proteins. The spliceosome, a large complex of RNA and proteins, facilitates two transesterification reactions that remove introns and ligate exons. RNA splicing generates protein diversity through alternative splicing and is important for cellular functions and disease processes.
transcription activators, repressors, & control RNA splicing, procesing and e...
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.post transcriptional modifications
This document summarizes post-transcriptional modifications in eukaryotes. It discusses how eukaryotic mRNA undergoes processing, including capping, splicing to remove introns, and polyadenylation. Splicing requires snRNPs and the spliceosome to recognize splice sites. Alternative splicing allows one gene to code for multiple proteins. tRNA and rRNA also undergo processing as they mature, including modification of bases and removal of sequences. Final mature mRNA, tRNA, and rRNA are then ready for translation.
POST TRANSCRIPTIONAL MODOFICATION.pptx
The document summarizes post-transcriptional modifications of RNA in eukaryotes. It describes how the primary transcript (hnRNA) undergoes processing to form mature mRNA through the addition of a 5' cap and 3' poly-A tail and splicing of introns. The 5' cap and 3' poly-A tail protect the mRNA from degradation. Splicing involves removing introns and joining exons, facilitated by interactions with small nuclear ribonucleoproteins and other proteins to form the spliceosome complex. This results in mRNA containing only the coding exons that can then be translated into protein.
Differential RNA Processing & Animal Development
1. Differential RNA processing regulates animal development through two major ways: nuclear RNA selection and differential RNA splicing.
2. Nuclear RNA selection involves selecting which nuclear transcripts are processed into cytoplasmic messenger RNA in different cell types.
3. Differential RNA splicing produces different mRNAs and proteins from the same nuclear RNA by using different combinations of exons through alternative splicing mechanisms like exon skipping, mutually exclusive exons, and alternate 5' or 3' splice sites.
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Post transcriptional modifications
- 1. Post transcriptional modifications Dr. Roshan Kumar Mahat (PhD Medical Biochemistry) Assistant Professor Department of Biochemistry
- 2. Objectives: 1. Processing of precursor mRNA 2. Processing of precursor rRNA 3. Processing of precursor tRNA 4. RNA editing
- 3. Processing of precursor mRNA Processing of mRNA from hnRNA includes: 1. Capping (5’cap) 2. Tailing (Polyadenylation) 3. Removal of extra RNA at 3’end 4. Splicing
- 4. Figure: Formation of the primary transcript and its processing during maturation of mRNA in a eukaryotic cell.
- 5. The 5’ cap of mRNA
- 6. Polyadenylation at 3’ end of mRNA
- 7. Splicing Splicing is the process of removal of introns and joining of exons to form functional mRNA. Classes of introns (4 classes): Group I Group II mRNA introns –spliceosome mediated splicing tRNA introns- requires endonuclease Self Splicing
- 8. Splicing of group I introns 1 2 1 2 21 Step-1 Step-2 Step-3
- 10. RNA pairing interactions in the formation of spliceosome complexes. The U1 snRNA has a sequence near its 5’ end that is complementary to the splice site at the 5’ end of the intron. Base pairing of U1 to this region of the primary transcript helps define the 5’ splice site during spliceosome assembly. U2 is paired to the intron at a position encompassing the A residue (shaded light red) that becomes the nucleophile during the splicing reaction. Spliceosome mediated splicing 5’ splice site 3’ splice siteBranch site
- 12. FIGURE: Overview of the processing of a eukaryotic mRNA.
- 13. Alternative splicing: • Alternative splicing allows synthesis of range of functionally distinct proteins from the primary transcript of a single gene. • Alternative splicing occurs by altering the patterns of exons from a single primary transcript.
- 14. Mechanisms of alternative splicing:
- 18. Disorders of splicing: 1. Beta thalassemia: The G-T sequence is mutated to A-T sequence resulting in defective RNA splicing. The defective β-globin mRNA can not be utilized for translation. 2. Systemic lupus erythematosus: Autoantibodies raised against U1 RNA of spliceosome.
- 19. Processing of precursor rRNA Posttranscriptional processing is not limited to mRNA. Ribosomal RNAs of bacterial, archaeal, and eukaryotic cells are made from longer precursors called preribosomal RNAs, or pre-rRNAs.
- 20. Figure: Processing of pre-rRNA transcripts in bacteria.
- 22. Figure: rRNA and ribosome synthesis
- 23. Processing of precursor tRNA The four different events of post- transcriptional processing of pre-tRNA molecules are as follows: 1. Removal of extra nucleotides from 5’ and 3’ ends 2. removal of intron from anticodon site 3. Modification of bases 4. Addition of CCA sequence
- 24. Figure: post transcriptional processing of tRNA RNAse P RNAse D Endonucleases RNA ligase 1 2 3 4 5 Nucleotidyl transferase
- 25. Fig: Overview of tRNA synthesis and its processing
- 26. RNA editing: Figure: RNA editing of apo-B pre mRNA