Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Lys34 of translation elongation factor EF-P is hydroxylated by YfcM

Peil, Lauri ; Starosta, Agata L ; Virumäe, Kai ; Atkinson, Gemma C LU ; Tenson, Tanel ; Remme, Jaanus and Wilson, Daniel N (2012) In Nature Chemical Biology 8. p.695-697
Abstract

Lys34 of the conserved translation elongation factor P (EF-P) is post-translationally lysinylated by YjeK and YjeA--a modification that is critical for bacterial virulence. Here we show that the currently accepted Escherichia coli EF-P modification pathway is incomplete and lacks a final hydroxylation step mediated by YfcM, an enzyme distinct from deoxyhypusine hydroxylase that catalyzes the final maturation step of eukaryotic initiation factor 5A, the eukaryotic EF-P homolog.

Please use this url to cite or link to this publication:
author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Chymotrypsin/chemistry, Escherichia coli/genetics, Escherichia coli Proteins/genetics, Gene Expression Regulation, Bacterial/physiology, Lysine/chemistry, Mass Spectrometry, Mixed Function Oxygenases/genetics, Molecular Structure, Peptide Elongation Factors/genetics, Protein Binding, Protein Processing, Post-Translational
in
Nature Chemical Biology
volume
8
pages
695 - 697
publisher
Nature Publishing Group
external identifiers
  • scopus:84864283412
  • pmid:22706199
ISSN
1552-4469
DOI
10.1038/nchembio.1001
language
English
LU publication?
no
id
6fea6ef3-6900-41d6-9d15-8ebc8789db06
date added to LUP
2021-09-27 15:55:18
date last changed
2024-04-20 13:11:39
@article{6fea6ef3-6900-41d6-9d15-8ebc8789db06,
  abstract     = {{<p>Lys34 of the conserved translation elongation factor P (EF-P) is post-translationally lysinylated by YjeK and YjeA--a modification that is critical for bacterial virulence. Here we show that the currently accepted Escherichia coli EF-P modification pathway is incomplete and lacks a final hydroxylation step mediated by YfcM, an enzyme distinct from deoxyhypusine hydroxylase that catalyzes the final maturation step of eukaryotic initiation factor 5A, the eukaryotic EF-P homolog.</p>}},
  author       = {{Peil, Lauri and Starosta, Agata L and Virumäe, Kai and Atkinson, Gemma C and Tenson, Tanel and Remme, Jaanus and Wilson, Daniel N}},
  issn         = {{1552-4469}},
  keywords     = {{Chymotrypsin/chemistry; Escherichia coli/genetics; Escherichia coli Proteins/genetics; Gene Expression Regulation, Bacterial/physiology; Lysine/chemistry; Mass Spectrometry; Mixed Function Oxygenases/genetics; Molecular Structure; Peptide Elongation Factors/genetics; Protein Binding; Protein Processing, Post-Translational}},
  language     = {{eng}},
  pages        = {{695--697}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Nature Chemical Biology}},
  title        = {{Lys34 of translation elongation factor EF-P is hydroxylated by YfcM}},
  url          = {{http://dx.doi.org/10.1038/nchembio.1001}},
  doi          = {{10.1038/nchembio.1001}},
  volume       = {{8}},
  year         = {{2012}},
}