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Redox proteomics of protein-bound methionine oxidation

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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.
Keywords
SEPSIS, DISEASES, PATHWAY, SULFOXIDE REDUCTASES, PEPTIDES, MECHANISM, ACTIVATION, FORCE-FIELD, ESCHERICHIA-COLI, ANTIOXIDANT DEFENSE

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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.
@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},
}

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