Chapter title |
Thioredoxin-Dependent Decomposition of Protein S-Nitrosothiols
|
---|---|
Chapter number | 22 |
Book title |
Nitric Oxide
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7695-9_22 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7694-2, 978-1-4939-7695-9
|
Authors |
Sophie Kneeshaw, Steven H. Spoel, Kneeshaw, Sophie, Spoel, Steven H. |
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. |
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Professor > Associate Professor | 1 | 17% |
Other | 0 | 0% |
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