Chapter title |
Identification of NO-Sensitive Cysteine Residues Using Cysteine Mutants of Recombinant Proteins
|
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Chapter number | 15 |
Book title |
Nitric Oxide
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7695-9_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7694-2, 978-1-4939-7695-9
|
Authors |
Azam Shekariesfahlan, Christian Lindermayr, Shekariesfahlan, Azam, Lindermayr, Christian |
Abstract |
Nitric oxide (NO) is a free radical gas regulating a wide range of biological processes in plants. Proteins are the main reaction target of NO inside the cells. The relevance of S-nitrosation as one of the NO-mediated protein posttranslational modifications has been studied in detail. S-nitrosylation causes alterations of the activity/function, sub-cellular localization or interaction partners of proteins. Up to present, a large number of S-nitrosation candidates have been detected in plants. Recombinant proteins are widely used to show or confirm the protein posttranslational modifications. Here, using recombinant proteins subjected to biotin switch assay, the S-nitrosation of some nuclear candidates of Arabidopsis is verified. Proteins usually contain several cysteine residues which each might involve in structure of protein active sites. So, an important question is: which cysteine residue is the target of S-nitrosation and does it belong to an active site? Here, using the approach of substitution of cysteines by serines on recombinant proteins, the NO-sensitive cysteine residue of an Arabidopsis nuclear protein is identified. The next step could be to investigate the effect of S-nitrosation on protein activity/function and further to test the role of target cysteines and S-nitrosation of them in protein activity/function. |
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