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A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P

Starosta, Agata L ; Lassak, Jürgen ; Peil, Lauri ; Atkinson, Gemma C LU ; Woolstenhulme, Christopher J ; Virumäe, Kai ; Buskirk, Allen ; Tenson, Tanel ; Remme, Jaanus and Jung, Kirsten , et al. (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.

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publishing date
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
2024-04-20 13:41:30
@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}},
}