Biology:Eukaryotic translation termination factor 1
 Generic protein structure example |
Eukaryotic translation termination factor 1 (eRF1), also known as TB3-1, is a protein that in humans is encoded by the ETF1 gene.[1][2][3]
In eukaryotes and archaea, this is the sole class 1 release factor (eRF) which recognizes all three stop codons. The overall process of termination is similar in bacteria, but in the latter 2 separate codon-recognizing release factors exist, RF1 and RF2. [4]
Function
Termination of protein biosynthesis and release of the nascent polypeptide chain are signaled by the presence of an in-frame stop codon at the aminoacyl site of the ribosome. The process of translation termination is universal and is mediated by protein release factors (RFs) and GTP. A class 1 RF recognizes the stop codon and promotes the hydrolysis of the ester bond linking the polypeptide chain with the peptidyl site tRNA, a reaction catalyzed at the peptidyl transferase center of the ribosome. Class 2 RFs, which are not codon specific and do not recognize codons, stimulate class 1 RF activity and confer GTP dependency upon the process. In bacteria, both class 1 RFs, RF1 and RF2, recognize UAA; however, UAG and UGA are decoded specifically by RF1 and RF2, respectively. In eukaryotes, eRF1, or ETF1, the functional counterpart of RF1 and RF2, functions as an omnipotent RF, decoding all 3 stop codons.[1][3]
References
- ↑ 1.0 1.1 "Entrez Gene: eukaryotic translation termination factor 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2107.
- ↑ "Chromosomal localization of a human cDNA containing a DIDS binding domain and demonstrating high homology to yeast omnipotent suppressor 45". Somat. Cell Mol. Genet. 18 (1): 97–102. January 1992. doi:10.1007/BF01233452. PMID 1546371.
- ↑ 3.0 3.1 "A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor". Nature 372 (6507): 701–3. December 1994. doi:10.1038/372701a0. PMID 7990965. Bibcode: 1994Natur.372..701F.
- ↑ "Termination of translation: interplay of mRNA, rRNAs and release factors?". EMBO J. 22 (2): 175–82. January 2003. doi:10.1093/emboj/cdg017. PMID 12514123.
Further reading
- "Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay". Genes Dev. 20 (3): 355–67. 2006. doi:10.1101/gad.1389006. PMID 16452507.
- "The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome". EMBO J. 21 (19): 5302–11. 2002. doi:10.1093/emboj/cdf484. PMID 12356746.
- "The effect of eukaryotic release factor depletion on translation termination in human cell lines". Nucleic Acids Res. 32 (15): 4491–502. 2004. doi:10.1093/nar/gkh791. PMID 15326224.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "[Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes]". Mol. Biol. (Mosk.) 42 (6): 1056–66. 2008. doi:10.1134/S0026893308060162. PMID 19140327.
- "Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3". Biochimie 88 (7): 747–57. 2006. doi:10.1016/j.biochi.2006.06.001. PMID 16797113.
- "Eukaryotic release factors (eRFs) history". Biol. Cell 95 (3–4): 195–209. 2003. doi:10.1016/S0248-4900(03)00035-2. PMID 12867083.
- "Does glutamine methylation affect the intrinsic conformation of the universally conserved GGQ motif in ribosomal release factors?". Biochemistry 48 (15): 3483–9. 2009. doi:10.1021/bi900117r. PMID 19265422.
- "Identification of a cellular factor that modulates HIV-1 programmed ribosomal frameshifting". J. Biol. Chem. 285 (26): 19776–84. 2010. doi:10.1074/jbc.M109.085621. PMID 20418372.
- "Defining the human deubiquitinating enzyme interaction landscape". Cell 138 (2): 389–403. 2009. doi:10.1016/j.cell.2009.04.042. PMID 19615732.
- "Downregulation of eRF1 by RNA interference increases mis-acylated tRNA suppression efficiency in human cells". Protein Eng. Des. Sel. 17 (12): 821–7. 2004. doi:10.1093/protein/gzh096. PMID 15716307.
- "Invariant amino acids essential for decoding function of polypeptide release factor eRF1". Nucleic Acids Res. 33 (19): 6418–25. 2005. doi:10.1093/nar/gki927. PMID 16282590.
- "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode: 2005Natur.433...77A.
- "HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1". FEBS Lett. 582 (16): 2352–6. 2008. doi:10.1016/j.febslet.2008.05.045. PMID 18539146.
- "Stop codons and UGG promote efficient binding of the polypeptide release factor eRF1 to the ribosomal A site". J. Mol. Biol. 331 (4): 745–58. 2003. doi:10.1016/S0022-2836(03)00813-1. PMID 12909007.
- "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm". EMBO J. 21 (22): 6205–15. 2002. doi:10.1093/emboj/cdf613. PMID 12426392.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. 2003. doi:10.1038/nbt810. PMID 12665801.
- "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases". Genes Dev. 21 (23): 3135–48. 2007. doi:10.1101/gad.1597707. PMID 18056425.
- "Eukaryotic class-1 translation termination factor eRF1: the NMR structure of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis". FEBS Journal 274 (16): 4223–37. 2007. doi:10.1111/j.1742-4658.2007.05949.x. PMID 17651434.
- "NMR Solution Structure and Function of the C-terminal Domain of Eukaryotic Polypeptide Release Factor eRF1". FEBS Journal 277 (12): 2611–27. 2010. doi:10.1111/j.1742-4658.2010.07672.x. PMID 20553496.
External links
- Termination+Release+Factor at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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