EMAIL THIS PAGE TO A FRIEND

Molecular & cellular proteomics : MCP

Redox proteomics of protein-bound methionine oxidation.


PMID 21406390

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.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

64430
DL-Methionine sulfoxide, ≥98.5% (NT)
C5H11NO3S
M1126
L-Methionine sulfoxide
C5H11NO3S