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Painting the Cysteine Chapel: New Tools to Probe Oxidation Biology
Author(s) -
Carroll Kate S
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.672.1
Subject(s) - sulfenic acid , cysteine , chemistry , biochemistry , cysteine metabolism , microbiology and biotechnology , computational biology , biology , enzyme
Oxidants are mediators of signaling pathways, where they modify proteins via chemoselective oxidation of redox sensitive cysteine residues. We have developed a chemical approach for selective detection of sulfenic acid‐modified proteins in living cells [ Mol Biosyst 2008]. Application of this new method to the discovery of protein targets of oxidation in mammalian cells has yielded identification of almost 200 proteins [ ACS Chem Biol 2009]. A small subset of these proteins is known to be oxidized in cells, but the majority of the proteins have not been previously characterized as oxidation targets. In addition, we have used this method to dissect the mechanism of peroxide sensing in yeast [ Chem Biol 2009] and to discover a periplasmic reducing system that protects single cysteines from oxidation [ Science 2009]. To further expand our capacity to investigate the dynamic sulfenome, we have also developed new immunochemical [ PNAS 2009] and ratiometric approaches. The ability to monitor cysteine oxidation in living cells opens new avenues for the rapidly expanding field of oxidation biology and we continue to develop these reagents for further study and application.