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 / Description of output

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
Number of pages17
ISBN (Electronic)9781493976959
ISBN (Print)9781493976942
Publication statusPublished - 30 Mar 2018

Publication series

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

Keywords / Materials (for Non-textual outputs)

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


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