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Describe Co- and post- translational modifications of proteins in ER in detail?
Anonymous
more than 3 weeks ago
Describe Co- and post- translational modifications of proteins in ER in detail?
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ChatGPT
more than 3 weeks ago
Co-translational modifications of proteins in the endoplasmic reticulum (ER) occur during the process of protein synthesis. As the protein is being synthesized by ribosomes on the rough ER membrane, it undergoes various modifications that help to ensure its proper folding and function. Some of the key co-translational modifications that occur in the ER include:
1. N-linked glycosylation: This is the attachment of a carbohydrate chain to an asparagine residue in the protein sequence. This modification helps to stabilize the protein structure and can also play a role in protein trafficking and sorting within the cell.
2. Disulfide bond formation: Disulfide bonds are covalent bonds between two cysteine residues in a protein that help to stabilize its structure. These bonds are formed in the ER lumen by enzymes called protein disulfide isomerases.
3. Signal peptide cleavage: Many proteins that are destined for secretion or insertion into the ER membrane contain a signal peptide at the N-terminus. This signal peptide is cleaved off during protein synthesis, allowing the protein to be properly targeted and localized within the cell.
Post-translational modifications of proteins in the ER occur after the protein has been fully synthesized and folded. These modifications can further regulate the protein's function, stability, and localization within the cell. Some of the key post-translational modifications that occur in the ER include:
1. Protein folding: Chaperone proteins in the ER help to ensure that newly synthesized proteins are properly folded into their functional three-dimensional structures. This process is critical for the proper function of the protein.
2. Protein glycosylation: In addition to N-linked glycosylation, proteins in the ER can also undergo O-linked glycosylation, where a carbohydrate chain is attached to a serine or threonine residue. This modification can play a role in protein stability and function.
3. Protein phosphorylation: Some proteins in the ER may undergo phosphorylation, where a phosphate group is added to a serine, threonine, or tyrosine residue. This modification can regulate the protein's activity and function.
Overall, co- and post-translational modifications of proteins in the ER play crucial roles in ensuring the proper folding, stability, and function of proteins within the cell. These modifications are tightly regulated processes that are essential for the proper functioning of the ER and the cell as a whole.
1. N-linked glycosylation: This is the attachment of a carbohydrate chain to an asparagine residue in the protein sequence. This modification helps to stabilize the protein structure and can also play a role in protein trafficking and sorting within the cell.
2. Disulfide bond formation: Disulfide bonds are covalent bonds between two cysteine residues in a protein that help to stabilize its structure. These bonds are formed in the ER lumen by enzymes called protein disulfide isomerases.
3. Signal peptide cleavage: Many proteins that are destined for secretion or insertion into the ER membrane contain a signal peptide at the N-terminus. This signal peptide is cleaved off during protein synthesis, allowing the protein to be properly targeted and localized within the cell.
Post-translational modifications of proteins in the ER occur after the protein has been fully synthesized and folded. These modifications can further regulate the protein's function, stability, and localization within the cell. Some of the key post-translational modifications that occur in the ER include:
1. Protein folding: Chaperone proteins in the ER help to ensure that newly synthesized proteins are properly folded into their functional three-dimensional structures. This process is critical for the proper function of the protein.
2. Protein glycosylation: In addition to N-linked glycosylation, proteins in the ER can also undergo O-linked glycosylation, where a carbohydrate chain is attached to a serine or threonine residue. This modification can play a role in protein stability and function.
3. Protein phosphorylation: Some proteins in the ER may undergo phosphorylation, where a phosphate group is added to a serine, threonine, or tyrosine residue. This modification can regulate the protein's activity and function.
Overall, co- and post-translational modifications of proteins in the ER play crucial roles in ensuring the proper folding, stability, and function of proteins within the cell. These modifications are tightly regulated processes that are essential for the proper functioning of the ER and the cell as a whole.
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Google Gemini AI
more than 3 weeks ago
Co- and Post-Translational Modifications of Proteins in the Endoplasmic Reticulum (ER)
Co-translational Modifications:
- Signal peptide cleavage: As the ribosome translates the mRNA, a signal peptide at the N-terminus of the nascent protein targets it to the ER. Once inside the ER, the signal peptide is cleaved by signal peptidase.
- N-linked glycosylation: Oligosaccharides are added to asparagine residues within the sequence Asn-Xaa-Ser/Thr (where Xaa is any amino acid except proline). This occurs on the lumenal side of the ER membrane by the oligosaccharyltransferase enzyme complex.
- Disulfide bond formation: Cysteine residues within the protein can form disulfide bonds with each other, creating disulfide bridges that stabilize the protein structure. This process is catalyzed by the enzyme protein disulfide isomerase (PDI).
Post-translational Modifications:
- Protein folding: The ER provides a folding environment for proteins. Chaperone proteins, such as BiP and GRP78, assist in the correct folding of newly synthesized proteins, preventing misfolding and aggregation.
- O-linked glycosylation: Oligosaccharides are added to serine or threonine residues on the lumenal or cytoplasmic side of the ER membrane. This type of glycosylation is typically found in proteoglycans and mucins.
- Hydroxylation of proline and lysine: Certain proline and lysine residues are hydroxylated by specific enzymes, such as prolyl hydroxylase and lysyl hydroxylase. These modifications are important for the stability and function of extracellular matrix proteins like collagen.
- Addition of GPI anchors: Glycophosphatidylinositol (GPI) anchors are added to proteins on the lumenal side of the ER membrane. GPI anchors allow proteins to be attached to the cell membrane without a transmembrane domain.
- Quality control: The ER has a quality control system to ensure that only properly folded and assembled proteins are released from the ER. Misfolded or unfolded proteins are retained in the ER and targeted for degradation by ubiquitination and proteasomal degradation.
Importance:
Co- and post-translational modifications in the ER are crucial for:
- Protein targeting and folding
- Stabilization and function of proteins
- Cell signaling and adhesion
- Extracellular matrix formation
- Protein quality control
Dysregulation of these modifications can lead to protein misfolding and aggregation, which is associated with various diseases, including neurodegenerative disorders and cancer.
Co-translational Modifications:
- Signal peptide cleavage: As the ribosome translates the mRNA, a signal peptide at the N-terminus of the nascent protein targets it to the ER. Once inside the ER, the signal peptide is cleaved by signal peptidase.
- N-linked glycosylation: Oligosaccharides are added to asparagine residues within the sequence Asn-Xaa-Ser/Thr (where Xaa is any amino acid except proline). This occurs on the lumenal side of the ER membrane by the oligosaccharyltransferase enzyme complex.
- Disulfide bond formation: Cysteine residues within the protein can form disulfide bonds with each other, creating disulfide bridges that stabilize the protein structure. This process is catalyzed by the enzyme protein disulfide isomerase (PDI).
Post-translational Modifications:
- Protein folding: The ER provides a folding environment for proteins. Chaperone proteins, such as BiP and GRP78, assist in the correct folding of newly synthesized proteins, preventing misfolding and aggregation.
- O-linked glycosylation: Oligosaccharides are added to serine or threonine residues on the lumenal or cytoplasmic side of the ER membrane. This type of glycosylation is typically found in proteoglycans and mucins.
- Hydroxylation of proline and lysine: Certain proline and lysine residues are hydroxylated by specific enzymes, such as prolyl hydroxylase and lysyl hydroxylase. These modifications are important for the stability and function of extracellular matrix proteins like collagen.
- Addition of GPI anchors: Glycophosphatidylinositol (GPI) anchors are added to proteins on the lumenal side of the ER membrane. GPI anchors allow proteins to be attached to the cell membrane without a transmembrane domain.
- Quality control: The ER has a quality control system to ensure that only properly folded and assembled proteins are released from the ER. Misfolded or unfolded proteins are retained in the ER and targeted for degradation by ubiquitination and proteasomal degradation.
Importance:
Co- and post-translational modifications in the ER are crucial for:
- Protein targeting and folding
- Stabilization and function of proteins
- Cell signaling and adhesion
- Extracellular matrix formation
- Protein quality control
Dysregulation of these modifications can lead to protein misfolding and aggregation, which is associated with various diseases, including neurodegenerative disorders and cancer.
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