A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl-tRNA drop-off |
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| Authors: | Yuya Watanabe Koichi Ito |
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| Institution: | a Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo (IMSUT), 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
b Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency (JST), Minato-ku, Tokyo 108-8639, Japan |
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| Abstract: | 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. |
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| Keywords: | Protein biosynthesis GTPase Premature peptidyl-tRNA drop-off Translation termination Polypeptide-chain release factor Ribosome function |
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