| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2048206 | FEBS Letters | 2010 | 5 Pages |
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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Authors
Yuya Watanabe, Yoshikazu Nakamura, Koichi Ito,