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Redox proteomics of protein-bound methionine oxidation

Bart Ghesquière UGent, Veronique Jonckheere UGent, Niklaas Colaert UGent, Joost Van Durme, Evy Timmerman UGent, Marc Goethals UGent, Joost Schymkowitz, Frederic Rousseau, Joël Vandekerckhove UGent and Kris Gevaert UGent (2011) MOLECULAR & CELLULAR PROTEOMICS. 10(5).
abstract
We here present a new method to measure the degree of protein-bound methionine sulfoxide formation at a proteome-wide scale. In human Jurkat cells that were stressed with hydrogen peroxide, over 2000 oxidation-sensitive methionines in more than 1600 different proteins were mapped and their extent of oxidation was quantified. Meta-analysis of the sequences surrounding the oxidized methionine residues revealed a high preference for neighboring polar residues. Using synthetic methionine sulfoxide containing peptides designed according to the observed sequence preferences in the oxidized Jurkat proteome, we discovered that the substrate specificity of the cellular methionine sulfoxide reductases is a major determinant for the steady-state of methionine oxidation. This was supported by a structural modeling of the MsrA catalytic center. Finally, we applied our method onto a serum proteome from a mouse sepsis model and identified 35 in vivo methionine oxidation events in 27 different proteins.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
SEPSIS, DISEASES, PATHWAY, SULFOXIDE REDUCTASES, PEPTIDES, MECHANISM, ACTIVATION, FORCE-FIELD, ESCHERICHIA-COLI, ANTIOXIDANT DEFENSE
journal title
MOLECULAR & CELLULAR PROTEOMICS
Mol. Cell. Proteomics
volume
10
issue
5
pages
12 pages
Web of Science type
Article
Web of Science id
000290216700019
JCR category
BIOCHEMICAL RESEARCH METHODS
JCR impact factor
7.398 (2011)
JCR rank
5/72 (2011)
JCR quartile
1 (2011)
ISSN
1535-9476
DOI
10.1074/mcp.M110.006866
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1887404
handle
http://hdl.handle.net/1854/LU-1887404
date created
2011-08-10 15:25:48
date last changed
2013-01-30 09:41:08
@article{1887404,
  abstract     = {We here present a new method to measure the degree of protein-bound methionine sulfoxide formation at a proteome-wide scale. In human Jurkat cells that were stressed with hydrogen peroxide, over 2000 oxidation-sensitive methionines in more than 1600 different proteins were mapped and their extent of oxidation was quantified. Meta-analysis of the sequences surrounding the oxidized methionine residues revealed a high preference for neighboring polar residues. Using synthetic methionine sulfoxide containing peptides designed according to the observed sequence preferences in the oxidized Jurkat proteome, we discovered that the substrate specificity of the cellular methionine sulfoxide reductases is a major determinant for the steady-state of methionine oxidation. This was supported by a structural modeling of the MsrA catalytic center. Finally, we applied our method onto a serum proteome from a mouse sepsis model and identified 35 in vivo methionine oxidation events in 27 different proteins.},
  author       = {Ghesqui{\`e}re, Bart and Jonckheere, Veronique and Colaert, Niklaas and Van Durme, Joost and Timmerman, Evy and Goethals, Marc and Schymkowitz, Joost and Rousseau, Frederic and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1535-9476},
  journal      = {MOLECULAR \& CELLULAR PROTEOMICS},
  keyword      = {SEPSIS,DISEASES,PATHWAY,SULFOXIDE REDUCTASES,PEPTIDES,MECHANISM,ACTIVATION,FORCE-FIELD,ESCHERICHIA-COLI,ANTIOXIDANT DEFENSE},
  language     = {eng},
  number       = {5},
  pages        = {12},
  title        = {Redox proteomics of protein-bound methionine oxidation},
  url          = {http://dx.doi.org/10.1074/mcp.M110.006866},
  volume       = {10},
  year         = {2011},
}

Chicago
Ghesquière, Bart, Veronique Jonckheere, Niklaas Colaert, Joost Van Durme, Evy Timmerman, Marc Goethals, Joost Schymkowitz, Frederic Rousseau, Joël Vandekerckhove, and Kris Gevaert. 2011. “Redox Proteomics of Protein-bound Methionine Oxidation.” Molecular & Cellular Proteomics 10 (5).
APA
Ghesquière, B., Jonckheere, V., Colaert, N., Van Durme, J., Timmerman, E., Goethals, M., Schymkowitz, J., et al. (2011). Redox proteomics of protein-bound methionine oxidation. MOLECULAR & CELLULAR PROTEOMICS, 10(5).
Vancouver
1.
Ghesquière B, Jonckheere V, Colaert N, Van Durme J, Timmerman E, Goethals M, et al. Redox proteomics of protein-bound methionine oxidation. MOLECULAR & CELLULAR PROTEOMICS. 2011;10(5).
MLA
Ghesquière, Bart, Veronique Jonckheere, Niklaas Colaert, et al. “Redox Proteomics of Protein-bound Methionine Oxidation.” MOLECULAR & CELLULAR PROTEOMICS 10.5 (2011): n. pag. Print.