Target type: biologicalprocess
Any process that modulates the frequency, rate or extent of translational termination. [GOC:go_curators]
Regulation of translational termination is a crucial step in protein synthesis, ensuring the accurate and efficient production of functional proteins. It involves the recognition and processing of stop codons within mRNA, triggering the disassembly of the ribosome and the release of the newly synthesized polypeptide chain.
**Key Players:**
* **Release Factors (RFs):** Proteins that bind to stop codons in the mRNA, signaling the end of translation. In eukaryotes, there are three main release factors: eRF1, eRF2, and eRF3.
* **Ribosome:** The molecular machinery responsible for protein synthesis. It has three main sites: the A (aminoacyl) site, the P (peptidyl) site, and the E (exit) site.
* **GTP:** Guanosine triphosphate, an energy source used in various cellular processes, including translation.
**Steps in the Process:**
1. **Stop Codon Recognition:** When the ribosome encounters a stop codon (UAA, UAG, or UGA) in the mRNA, it pauses translation.
2. **Release Factor Binding:** eRF1, the primary release factor, binds to the stop codon in the A site of the ribosome. eRF2, a GTPase, interacts with eRF1, facilitating its function.
3. **Peptide Chain Release:** eRF1 interacts with the peptidyl transferase center of the ribosome, stimulating the hydrolysis of the bond between the polypeptide chain and the tRNA in the P site. This releases the newly synthesized protein.
4. **Ribosome Dissociation:** eRF1 and eRF2, along with GTP hydrolysis, trigger the disassembly of the ribosome. The ribosomal subunits (40S and 60S in eukaryotes) dissociate, ready for another round of translation.
5. **Recycling of Ribosomal Components:** The released ribosomal subunits, tRNAs, and release factors are recycled for subsequent rounds of protein synthesis.
**Regulation of Translational Termination:**
* **Regulation of Release Factor Activity:** The activity of release factors can be regulated by various mechanisms, including phosphorylation, ubiquitination, and interaction with other proteins.
* **mRNA Structure and Sequence:** The sequence surrounding the stop codon can influence the efficiency of termination. Some mRNA sequences can promote premature termination, leading to the production of truncated proteins.
* **Stress Response:** Cellular stress conditions, such as heat shock or nutrient deprivation, can affect the regulation of translation termination. This may involve altering the activity of release factors or modifying mRNA stability.
**Consequences of Dysregulation:**
* **Errors in Protein Synthesis:** Dysregulation of translational termination can lead to the production of incomplete or misfolded proteins, which can have detrimental effects on cellular function.
* **Disease Development:** Defects in translational termination have been linked to various diseases, including cancer, neurodegenerative disorders, and genetic disorders.
**In conclusion, the regulation of translational termination is a tightly controlled process crucial for maintaining the accuracy and efficiency of protein synthesis. It involves a complex interplay of release factors, ribosomes, and other cellular components. Dysregulation of this process can have significant consequences for cellular function and health.**'
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Protein | Definition | Taxonomy |
---|---|---|
Prolyl 3-hydroxylase OGFOD1 | A prolyl 3-hydroxylase OGFOD1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8N543] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
fg-4592 | roxadustat : An N-acylglycine resulting from the formal condensation of the amino group of glycine with the carboxy group of 4-hydroxy-1-methyl-7-phenoxyisoquinoline-3-carboxylic acid. It is an inhibitor of hypoxia inducible factor prolyl hydroxylase (HIF-PH). roxadustat: structure in first source | aromatic ether; isoquinolines; N-acylglycine | EC 1.14.11.2 (procollagen-proline dioxygenase) inhibitor; EC 1.14.11.29 (hypoxia-inducible factor-proline dioxygenase) inhibitor |
bay 85-3934 |