ArticleRNA (New York, N.Y.)2000
The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246.
Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Codon reassignment to facilitate genetic engineering and biocontainment in the chloroplast of Chlamydomonas reinhardtii.Plant biotechnology journal · 2016Article
- A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.Nature structural & molecular biology · 2012Article
- The codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop.RNA (New York, N.Y.) · 2010Article
- Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria.RNA (New York, N.Y.) · 2010Article
- Mitochondrial release factor in yeast: interplay of functional domains.Current genetics · 2008Article
- An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination.Nucleic acids research · 2007Article
- Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms.Nucleic acids research · 2006Article
- Common and specific amino acid residues in the prokaryotic polypeptide release factors RF1 and RF2: possible functional implications.Nucleic acids research · 2005Article
- HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- A dynamic competition between release factor 2 and the tRNA(Sec) decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H.The EMBO journal · 2001Article
- Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition.Nucleic acids research · 2001Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replacing a cassette of 31 residues from Escherichia coli release factor 1 with the equivalent residues in release factor 2 gave a protein active in codon-specific binding to the ribosome but inactive in peptidyl-tRNA hydrolysis. Such a phenotype is also found unexpectedly with release factor 2 when expressed at high concentration in bacteria. Substituting threonine with the release factor 1 equivalent serine at position 246 within the cassette restored the impaired activity of the chimeric protein, and also that of inactive recombinant release factor 2, both in vitro and in vivo. The differences in activity are not due to posttranslational modifications or a lack of it at this residue. Random mutagenesis of codon 246 suggests that this position is pivotal for the function of the release factor, being able to affect differentially both its binding to the ribosome and its peptide release activities. We propose that amino acid 246 is close to a sharp turn (GGQ motif at position 250), and is essential for transmitting the signal from cognate codon recognition by correctly positioning the peptidyl-tRNA hydrolysis domain of the release factor into the peptidyltransferase center.
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