Unbiased identification of cysteine S-nitrosylation sites on proteins View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-06-28

AUTHORS

Behrad Derakhshan, Pamela C Wille, Steven S Gross

ABSTRACT

Covalent addition of nitric oxide (NO) to Cys-sulfur in proteins, or S-nitrosylation, plays pervasive roles in the physiological and pathophysiological modulation of mammalian protein functions. Knowledge of the specific protein Cys residues that undergo NO addition in different biological settings is fundamental to understanding NO-mediated signal transduction. Here, we describe in detail an MS-based proteomic protocol for facile, high-throughput and unbiased discovery of SNO-Cys residues in proteins from complex biological samples. The approach, termed SNOSID (SNO-Cys site identification), can be used to identify endogenous and chemically induced S-nitrosylation sites in proteins from tissues or cells. Identified SNO-Cys sites may provide insights into novel mechanisms and proteins that mediate NO bioactivities in health and disease. SNOSID builds on the biotin-switch method for covalent addition of disulfide-linked biotin at S-nitrosylation sites on proteins. Biotinylated proteins are then subjected to trypsinolysis and the resulting biotin-tagged peptides are affinity-captured on streptavidin-agarose. After selective elution with β-mercaptoethanol, the peptides are sequenced using nanoflow liquid chromatography tandem mass spectrometry (nLC-MS/MS). Validation that identified peptide ions as originating from authentic NO-Cys-containing precursor proteins can be provided by establishing that these peptide ions are absent from control samples where S–NO bonds were subjected to prior photolysis, using a UV transilluminator. The protocol requires approximately 2 days for sample processing, including the incubation time for proteolysis. An additional 1–2 days is needed for sample analysis by nLC-MS/MS and data analysis/interpretation. More... »

PAGES

1685-1691

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nprot.2007.210

DOI

http://dx.doi.org/10.1038/nprot.2007.210

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025395108

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17641633


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