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 | 
|---|---|
| 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 | 
		
	
