A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P
(2014) In Cell Reports 9(2). p.476-483- 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... (More)
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.
(Less)
- author
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- keywords
- Amino Acid Sequence, Conserved Sequence, Escherichia coli/chemistry, Escherichia coli Proteins/chemistry, Evolution, Molecular, Molecular Sequence Data, Mutation, Peptide Elongation Factors/chemistry, Peptides/genetics, Valine-tRNA Ligase/chemistry
- in
- Cell Reports
- volume
- 9
- issue
- 2
- pages
- 476 - 483
- publisher
- Cell Press
- external identifiers
-
- scopus:84919876711
- pmid:25310979
- ISSN
- 2211-1247
- DOI
- 10.1016/j.celrep.2014.09.008
- language
- English
- LU publication?
- no
- id
- a0e31302-865a-4968-a8a6-f4758c427c0d
- date added to LUP
- 2021-09-27 15:53:22
- date last changed
- 2024-06-29 18:40:28
@article{a0e31302-865a-4968-a8a6-f4758c427c0d, abstract = {{<p>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. </p>}}, author = {{Starosta, Agata L and Lassak, Jürgen and Peil, Lauri and Atkinson, Gemma C and Woolstenhulme, Christopher J and Virumäe, Kai and Buskirk, Allen and Tenson, Tanel and Remme, Jaanus and Jung, Kirsten and Wilson, Daniel N}}, issn = {{2211-1247}}, keywords = {{Amino Acid Sequence; Conserved Sequence; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Evolution, Molecular; Molecular Sequence Data; Mutation; Peptide Elongation Factors/chemistry; Peptides/genetics; Valine-tRNA Ligase/chemistry}}, language = {{eng}}, number = {{2}}, pages = {{476--483}}, publisher = {{Cell Press}}, series = {{Cell Reports}}, title = {{A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P}}, url = {{http://dx.doi.org/10.1016/j.celrep.2014.09.008}}, doi = {{10.1016/j.celrep.2014.09.008}}, volume = {{9}}, year = {{2014}}, }