Analysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique

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TitreAnalysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique
Type de publicationBook Chapter
Year of Publication2018
AuteursAime SEB, Hichami S, Wendehenne D, Lamotte O
EditorMengel A, Lindermayr C
Book TitleNITRIC OXIDE: Methods and Protocols
Series TitleMethods in Molecular Biology
Volume1747
Pagination131-141
PublisherHUMANA PRESS INC
City999 RIVERVIEW DR, STE 208, TOTOWA, NJ 07512-1165 USA
ISBN Number978-1-4939-7695-9; 978-1-4939-7694-2
ISBN1064-3745
Mots-clésBiotin switch, Nitric oxide, Recombinant protein, Redox-based posttranslational modification, S-nitrosation, S-nitrosothiols, S-nitrosylation
Résumé

Nitric oxide is regarded as a key signaling messenger in several organisms. Its physiological relevance is partly due to its capacity to induce posttranslational modifications of proteins through its direct or indirect reaction with specific amino acid residues. Among them, S-nitrosylation has been shown to be involved in a broad range of cellular signaling pathways both in animals and plants. The identification of S-nitrosylated proteins has been made possible by the development of the Biotin-Switch Technique (BST) in the early 2000s. Here, we describe the BST protocol we routinely use to check in vitro S-nitrosylation of recombinant proteins induced by NO donors.

DOI10.1007/978-1-4939-7695-9_11