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Identification of S-nitrosylated proteins in plants.
Methods Enzymol. 440, 283-293 (2008)
Posttranslational protein modifications affect the function or the activity of proteins and exhibit important mechanisms in regulating cellular events. A broad spectrum of modifications is known, including redox-dependent alterations. During the last decade, covalent binding of nitric oxide (NO) to protein cysteines, termed S-nitrosylation, seems especially an evident process for redox-related signaling. To reveal potential target proteins for S-nitrosylation, the biotin switch method gains more and more in importance. This technique is a tool used for analyzing the nitrosylome as well as the examination of single candidates. It is based on substitution of the NO group by a biotin linker that simplifies the detection and the purification of recently S-nitrosylated proteins in a three-step procedure.
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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0076-6879
e-ISSN
0076-6879
Journal
Methods in Enzymology
Quellenangaben
Volume: 440,
Pages: 283-293
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Biochemical Plant Pathology (BIOP)