Identification of S-nitrosylated proteins in plants

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

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.

Publication types

  • Review

MeSH terms

  • Nitrosation
  • Plant Proteins / analysis*
  • Plant Proteins / chemistry
  • Plant Proteins / classification
  • Plant Proteins / metabolism*
  • Plants / chemistry
  • Plants / metabolism*
  • S-Nitrosothiols / analysis*
  • S-Nitrosothiols / chemistry
  • S-Nitrosothiols / classification
  • S-Nitrosothiols / metabolism*

Substances

  • Plant Proteins
  • S-Nitrosothiols