Eukaryotic release factors

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Eukaryotic translation termination factor 1
ERF1.png
Ribbon diagram of human eukaryotic release factor 1.[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ETF1 ; D5S1995; ERF; ERF1; RF1; SUP45L1; TB3-1
External IDs OMIM600285 MGI2385071 HomoloGene3475 GeneCards: ETF1 Gene
Orthologs
Species Human Mouse
Entrez 2107 225363
Ensembl ENSG00000120705 ENSMUSG00000024360
UniProt P62495 Q8BWY3
RefSeq (mRNA) NM_004730 NM_144866
RefSeq (protein) NP_004721 NP_659115
Location (UCSC) Chr 5:
137.84 – 137.88 Mb
Chr 18:
34.9 – 34.93 Mb
PubMed search [1] [2]


Eukaryotic translation termination factor 1 (eRF1), also known asTB3-1, is a protein that in humans is encoded by the ETF1 gene.[2][3][4]

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.[5]

Function[edit]

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.[2][4]

References[edit]

  1. ^ PDB 1DT9; 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". Cell 100 (3): 311–21. doi:10.1016/S0092-8674(00)80667-4. PMID 10676813. ; rendered via PyMOL
  2. ^ a b "Entrez Gene: eukaryotic translation termination factor 1". 
  3. ^ 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. PMID 1546371. 
  4. ^ a b Frolova 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". Nature 372 (6507): 701–3. doi:10.1038/372701a0. PMID 7990965. 
  5. ^ Kisselev L, Ehrenberg M, Frolova L (January 2003). "Termination of translation: interplay of mRNA, rRNAs and release factors?". EMBO J. 22 (2): 175–82. doi:10.1093/emboj/cdg017. PMC 140092. PMID 12514123. 


Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.