Lys34 of translation elongation factor EF-P is hydroxylated by YfcM
(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.
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https://lup.lub.lu.se/record/6fea6ef3-6900-41d6-9d15-8ebc8789db06
- author
- Peil, Lauri ; Starosta, Agata L ; Virumäe, Kai ; Atkinson, Gemma C LU ; Tenson, Tanel ; Remme, Jaanus and Wilson, Daniel N
- publishing date
- 2012-08
- 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
- 2024-06-15 17:08:17
@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}}, }