Biotin switch processing and mass spectrometry analysis of S-nitrosated thioredoxin and its transnitrosation targets

Changgong Wu, Tong Liu, Yan Wang, Lin Yan, Chuanlong Cui, Annie Beuve, Hong Li

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

S-Nitrosation is a key posttranslational modification in regulating proteins in both normal physiology and diverse human diseases. To identify novel therapies for human diseases linked to oxidative and nitrosative stress, understanding how cells control S-nitrosation specificity could be critical. Among the enzymes known to control S-nitrosation of proteins, thioredoxin 1 (Trx1), a conserved disulfide reductase, transnitrosates and denitrosates distinct sets of target proteins. To recognize the function of Trx1 in both normal and dysfunctional cells, S-nitrosation targets of Trx1 in different cells need to be identified. However, S-nitrosation is usually too labile to be detected directly by mass spectrometry (MS). Here we present two optimized MS techniques to identify S-nitrosated Trx1 and its transnitrosation targets, using both direct and indirect MS methods.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages253-266
Number of pages14
DOIs
StatePublished - 2018

Publication series

NameMethods in Molecular Biology
Volume1747
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Keywords

  • Mass spectrometry
  • S-nitrosation
  • Thioredoxin
  • Transnitrosation

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