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Methods Enzymol. 2008;440:283-93. doi: 10.1016/S0076-6879(07)00818-X.

Identification of S-nitrosylated proteins in plants.

Author information

1
Institute of Biochemical Plant Pathology, Helmholtz Zentrum M√ľnchen, German Research Center for Environmental Health, Munich-Neuherberg, Germany.

Abstract

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.

PMID:
18423225
DOI:
10.1016/S0076-6879(07)00818-X
[Indexed for MEDLINE]

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