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A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl‐tRNA drop‐off
Author(s) -
Watanabe Yuya,
Nakamura Yoshikazu,
Ito Koichi
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.12.048
Subject(s) - transfer rna , drop (telecommunication) , translation (biology) , protein biosynthesis , release factor , nucleotide , biology , mutation , biophysics , genetics , chemistry , rna , gene , messenger rna , telecommunications , computer science
The bacterial translation factor RF3 promotes translation termination by recycling the tRNA‐mimicking release factors, RF1 and RF2, after mature polypeptide release. RF3 also enhances the premature peptidyl‐tRNA drop‐off reaction in the presence of RRF and EF‐G. Despite the recently resolved X‐ray crystal structure of RF3, the molecular details of the bimodal functionality of RF3 remain obscure. In this report, we demonstrate a novel class of RF3 mutations specifically defective in the tRNA drop‐off reaction. These mutations suggest differential molecular pathways closely related to the guanine nucleotide modes of RF3.