Abstract
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.
Dokumententyp: | Zeitschriftenartikel |
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Fakultät: | Biologie > Department Biologie I |
Themengebiete: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie |
URN: | urn:nbn:de:bvb:19-epub-33392-1 |
ISSN: | 2211-1247 |
Sprache: | Englisch |
Dokumenten ID: | 33392 |
Datum der Veröffentlichung auf Open Access LMU: | 15. Feb. 2017, 14:44 |
Letzte Änderungen: | 04. Nov. 2020, 13:11 |