| Literature DB >> 22975312 |
Kiyohito Kihira1, Yoshihiro Shimizu, Yasuhito Shomura, Naoki Shibata, Masaya Kitamura, Atsushi Nakagawa, Takuya Ueda, Kozo Ochi, Yoshiki Higuchi.
Abstract
The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3',5'-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.Entities:
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Year: 2012 PMID: 22975312 DOI: 10.1016/j.febslet.2012.08.029
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124