Journal
CHEMISTRY & BIOLOGY
Volume 9, Issue 12, Pages 1329-1335Publisher
CELL PRESS
DOI: 10.1016/S1074-5521(02)00293-4
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Funding
- NIDA NIH HHS [DA00074] Funding Source: Medline
- NIMH NIH HHS [MH-18501, R01 MH066204-01, R01 MH066204, MH-66204] Funding Source: Medline
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S-Nitrosylation of specific cysteine residues is a reversible signaling mechanism of nitric oxide (NO) generated by NO synthase (NOS) enzymes. In some proteins, evidence has accumulated that more than one cysteine can be S-nitrosylated; however, it is difficult to distinguish S-nitrosylation on separate cysteine residues. We report a novel simple, sensitive, and specific procedure for nitrosopeptide mapping. Dexras1 is a monomeric G protein whose guanine nucleotide exchange activity is augmented by NO; the identity and number of its S-nitrosylated cysteines is unknown. We describe the radiolabeling of S-nitrosylated cysteine residues in Dexras1. A nitrosopeptide map, generated by two-dimensional peptide chromatography, reveals that only a single cysteine is S-nitrosylated following NO exposure. Mutagenesis of Cys11 abolished the effect of NO donors on Dexras1, implicating this residue in the NO-mediated activation of Dexras1.
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