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PMID: 12189178 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1.

EMBO reports ·Vol. 3 ·No. 9 ·2002-09-00 ·Pages 881-6

Seit-Nebi A, Frolova L, Kisselev L

Abstract

In eukaryotic ribosomes, termination of translation is triggered by class 1 polypeptide release factor, eRF1. In organisms with a universal code, eRF1 responds to three stop codons, whereas, in ciliates with variant codes, only one or two codon(s) remain(s) as stop signals. By mutagenesis of the Y-C-F minidomain of the N domain, we converted an omnipotent human eRF1 recognizing all three stop codons into a unipotent 'ciliate-like' UGA-only eRF1. The conserved Cys127 located in the Y-C-F minidomain plays a critical role in stop codon recognition. The UGA-only response has also been achieved by concomitant substitutions of four other amino acids located at the Y-C-F and NIKS minidomains of eRF1. We suggest that for eRF1 the stop codon decoding is of a non-linear (non-protein-anticodon) type and explores a combination of positive and negative determinants. We assume that stop codon recognition is profoundly different by eukaryotic and prokaryotic class 1 RFs.

MeSH Terms
Amino Acid Sequence Animals Codon Cysteine/chemistry DNA, Complementary/metabolism Humans Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Peptide Termination Factors/chemistry,metabolism Protein Conformation Protein Structure, Tertiary Ribosomes/metabolism Sequence Homology, Amino Acid
Chemicals
Codon DNA, Complementary ETF1 protein, human Peptide Termination Factors Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Seit-Nebi Alim
Engelhardt Institute of Molecular Biology, Moscow, Russia.
Frolova Ludmila
Kisselev Lev
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27 references, click to expand
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Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-221X
DOI
10.1093/embo-reports/kvf178
Published
2002-09-00
Epub
2002-00-16
Pages
881-6
Language
English
Region
England
NLM ID
100963049
PMCID
PMC1084231
Subset
IM
External Links
PubMed source DOI: 10.1093/embo-reports/kvf178 PMC Full Text View journal details
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