Eukaryotic translation termination factor 1 (eRF1), also known asTB3-1, is a protein that in humans is encoded by the ETF1gene.
In eukaryotes, this is the only release factor (eRF) which recognizes all three stop codons. The overall process of termination is similar in prokaryotes, but in the latter 3 separate release factors exist, RF1, RF and RF3, each recognizing one of the 3 stop codons.
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 prokaryotes, 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.
^PDB1DT9; Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D (February 2000). "The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis". Cell100 (3): 311–21. doi:10.1016/S0092-8674(00)80667-4. PMID10676813.; rendered via PyMOL
^Grenett HE, Eipers PG, Kidd VJ, Bounelis P, Fuller GM (January 1992). "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. doi:10.1007/BF01233452. PMID1546371.
^ abFrolova L, Le Goff X, Rasmussen HH, Cheperegin S, Drugeon G, Kress M, Arman I, Haenni AL, Celis JE, Philippe M (December 1994). "A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor". Nature372 (6507): 701–3. doi:10.1038/372701a0. PMID7990965.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Ivanova EV, Alkalaeva EZ, Birsdall B et al. (2008). "[Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes]". Mol. Biol. (Mosk.)42 (6): 1056–66. PMID19140327.
Ilegems E, Pick HM, Vogel H (2004). "Downregulation of eRF1 by RNA interference increases mis-acylated tRNA suppression efficiency in human cells". Protein Eng. Des. Sel.17 (12): 821–7. doi:10.1093/protein/gzh096. PMID15716307.
Chavatte L, Frolova L, LaugÃ¢a P et al. (2003). "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. doi:10.1016/S0022-2836(03)00813-1. PMID12909007.
Gevaert K, Goethals M, Martens L et al. (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol.21 (5): 566–9. doi:10.1038/nbt810. PMID12665801.
Ivanova EV, Kolosov PM, Birdsall B (2007). "Eukaryotic class-1 translation termination factor eRF1: the NMR structure of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis". FEBS Journal274 (16): 4223–37. doi:10.1111/j.1742-4658.2007.05949.x. PMID17651434.
Mantsyzov AB, Ivanova EV, Birdsall B (2010). "NMR Solution Structure and Function of the C-terminal Domain of Eukaryotic Polypeptide Release Factor eRF1". FEBS Journal277 (12): 2611–27. doi:10.1111/j.1742-4658.2010.07672.x. PMID20553496.