Functional proteomics approaches for the identification of transnitrosylase and denitrosylase targets

Changgong Wu, Andrew Myles Parrott, Tong Liu, Annie Beuve, Hong Li

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Protein S-nitrosylation is a dynamic post-translational modification (PTM) of specific cysteines within a target protein. Both proteins and small molecules are known to regulate the attachment and removal of this PTM, and proteins exhibiting such a function are transnitrosylase or denitrosylase candidates. With the advent of the biotin switch technique coupled to high-throughput proteomics workflows, the identification and quantification of large numbers of S-nitrosylated proteins and peptides is now possible. Proper analysis and interpretation of high throughout and quantitative proteomics data will help identify specific transnitrosylase and denitrosylase target peptide sequences and contribute to an understanding of the function and regulation of specific S-nitrosylation events. Here we describe the application of a quantitative proteomics approach using isotope-coded affinity tags (ICAT) in the biotin switch approach for the identification of transnitrosylation and denitrosylation targets of thioredoxin 1, an enigmatic protein with both reported transnitrosylase and denitrosylase activities.

Original languageEnglish (US)
Pages (from-to)151-160
Number of pages10
JournalMethods
Volume62
Issue number2
DOIs
StatePublished - Aug 1 2013

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Keywords

  • Biotin switch
  • ICAT
  • Proteomics
  • S-nitrosylation
  • Thioredoxin

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