Endogenous S-nitrosocysteine proteomic inventories identify a core of proteins in heart metabolic pathways.

ABSTRACT: Protein cysteine residues are essential for protein folding, participate in enzymatic catalysis, and coordinate the binding of metal ions to proteins. Enzymatically catalyzed and redox-dependent post-translational modifications of cysteine residues are also critical for signal transduction and regulation of protein function and localization. S-nitrosylation, the addition of a nitric oxide equivalent to a cysteine residue, is a redox-dependent modification. In this study, we curated and analyzed four different studies that employed various chemoselective platforms coupled to mass spectrometry to precisely identify S-nitrosocysteine residues in mouse heart proteins. Collectively 1974 S-nitrosocysteine residues in 761 proteins were identified and 33.4% were identified in two or more studies.

SUBMITTER: Lau B 

PROVIDER: S-EPMC8497991 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature