期刊
CELL REPORTS
卷 9, 期 2, 页码 476-483出版社
CELL PRESS
DOI: 10.1016/j.celrep.2014.09.008
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资金
- Deutsche Forschungsgemeinschaft [FOR1805, WI3285/4-1, Exc114/2]
- Estonian Science Foundation [ETF9020, IUT 14021]
- European Social Fund program [MJD144, MJD99]
- AXA Research Fund
- Marie Curie
Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyproline stretches in proteins. We have discovered that only a single polyproline stretch is invariant across all domains of life, namely a proline triplet in ValS, the tRNA synthetase, that charges tRNA(Val) with valine. Here, we show that expression of ValS in vivo and in vitro requires EF-P and demonstrate that the proline triplet located in the active site of ValS is important for efficient charging of tRNA(Val) with valine and preventing formation of mischarged Thr-tRNA(Val) as well as efficient growth of E. coli in vivo. We suggest that the critical role of the proline triplet for ValS activity may explain why bacterial cells coevolved the EF-P rescue system.
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