PMID: 11911360Mar 26, 2002Paper

Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1

RNA
Ludmila FrolovaLev Kisselev

Abstract

Class-1 polypeptide chain release factors (RFs) play a key role in translation termination. Eukaryotic (eRF1) and archaeal class-1 RFs possess a highly conserved Asn-Ile-Lys-Ser (NIKS) tetrapeptide located at the N-terminal domain of human eRF1. In the three-dimensional structure, NIKS forms a loop between helices. The universal occurrence and exposed nature of this motif provoke the appearance of hypotheses postulating an essential role of this tetrapeptide in stop codon recognition and ribosome binding. To approach this problem experimentally, site-directed mutagenesis of the NIKS (positions 61-64) in human eRF1 and adjacent amino acids has been applied followed by determination of release activity and ribosome-binding capacity of mutants. Substitutions of Asn61 and Ile62 residues of the NIKS cause a decrease in the ability of eRF1 mutants to promote termination reaction in vitro, but to a different extent depending on the stop codon specificity, position, and nature of the substituting residues. This observation points to a possibility that Asn-Ile dipeptide modulates the specific recognition of the stop codons by eRF1. Some replacements at positions 60, 63, and 64 cause a negligible (if any) effect in contrast to what has b...Continue Reading

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Citations

May 5, 2005·Journal of Molecular Evolution·Han LiangLaura F Landweber
Feb 11, 2003·Trends in Biochemical Sciences·Yoshikazu Nakamura, Koichi Ito
May 31, 2011·Nature Structural & Molecular Biology·Thomas BeckerRoland Beckmann
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Jan 7, 2003·The EMBO Journal·Lev KisselevLudmila Frolova
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Oct 3, 2009·FEBS Letters·Elena AlkalaevaLev Kisselev

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