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Updated: Jun 17, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature
Yuya Watanabe1, Yoshikazu Nakamura, Koichi Ito
1Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo (IMSUT), Tokyo, Japan.
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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