Thioredoxin-Dependent Decomposition of Protein S-Nitrosothiols

Sophie Kneeshaw, Steven H Spoel

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

Abstract

The addition of nitric oxide to cysteine moieties of proteins results in the formation of S-nitrosothiols (SNO) that have emerged as important posttranslational signaling cues in a wide variety of eukaryotic processes. While formation of protein-SNO is largely nonenzymatic, the conserved family of Thioredoxin (TRX) enzymes are capable of selectively reducing protein-SNO. Consequently, TRX enzymes are thought to provide reversibility and specificity to protein-SNO signaling networks. Here, we describe an in vitro methodology based on enzymatic oxidoreductase and biotin-switch techniques, allowing for the detection of protein-SNO targets of TRX enzymes. We show that this methodology identifies both global and specific protein-SNO targets of TRX in plant cell extracts.
Original languageEnglish
Title of host publicationNitric Oxide
Subtitle of host publicationMethods and Protocols
EditorsAlexander Mengel, Christian Lindermayr
PublisherHUMANA PRESS INC
Pages281-297
Number of pages17
Volume1747
ISBN (Electronic)9781493976959
ISBN (Print)9781493976942
DOIs
Publication statusPublished - 30 Mar 2018

Publication series

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

Keywords

  • Biotin Switch Technique
  • S-nitrosylation
  • denitrosylation
  • Thioredoxin
  • Protein-SNO Reductase,
  • Nitric Oxide

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