期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms11657
关键词
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资金
- Japan Science and Technology Agency (JST) PRESTO of Molecular Technology and Creation of New Functions
- JST CREST Rising Star Award of Molecular Technology
- JSPS [26560429]
- JST CREST of Molecular Technologies
- Japan Society for the Promotion of Science (JSPS) [26220204]
- Max Planck Society
- Deutsche Forschungsgemeinschaft [FOR 1805]
- Grants-in-Aid for Scientific Research [26220204, 26560429] Funding Source: KAKEN
The ribosome stalls on translation of polyproline sequences due to inefficient peptide bond formation between consecutive prolines. The translation factor EF-P is able to alleviate this stalling by accelerating Pro-Pro formation. However, the mechanism by which EF-P recognizes the stalled complexes and accelerates peptide bond formation is not known. Here, we use genetic code reprogramming through a flexible in-vitro translation (FIT) system to investigate how mutations in tRNA(Pro) affect EF-P function. We show that the 9-nt D-loop closed by the stable D-stem sequence in tRNA(Pro) is a crucial recognition determinant for EF-P. Such D-arm structures are shared only among the tRNA(Pro) isoacceptors and tRNA(fMet) in Escherichia coli, and the D-arm of tRNA(fMet) is essential for EF-P-induced acceleration of fMet-puromycin formation. Thus, the activity of EF-P is controlled by recognition elements in the tRNA D-arm.
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