title: Identification of S-nitrosylated proteins in plants.
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.
authors.affiliation: Institute of Biochemical Plant Pathology, Helmholtz Zentrum München, German Research Center for Environmental Health, Munich-Neuherberg, Germany.
authors.forename: Simone
authors.initials: S
authors.lastname: Sell
authors.forename: Christian
authors.initials: C
authors.lastname: Lindermayr
authors.forename: Jörg
authors.initials: J
authors.lastname: Durner
mesh_terms: D015538:Nitrosation; D010940:Plant Proteins / Q000032:analysis* / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D010944:Plants / Q000737:chemistry / Q000378:metabolism*; D026403:S-Nitrosothiols / Q000032:analysis* / Q000737:chemistry / Q000145:classification / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D026403:S-Nitrosothiols