Résumé
Over the last decade, due to its broad biological effects, nitric oxide (NO) has triggered a huge interest in the plant science too. Nitrosylation of cystein thiol residues (SNO) in proteins has been shown to be the main target of endogenously produced NO or in a biological sample exposed to this gas. This chapter summarizes the hitherto 18 different methods developed to identify and quantify nitrosylated proteins. These methods derive mostly from the original “Biotin-Switch” technique (BS) published in 2001 but new approaches try to circumvent BS weaknesses. Surprisingly, out of this bloomy panel only a couple of methods have been used in plants. By collecting all the plant published data up to now, we “blasted” them against the proteome of the plant model Arabidopsis and identified 373 nonredundant nitrosylated proteins. We then provide the first overview of plant nitrosylated proteome showing a wide range of functions and cellular compartments involved in NO signaling/targeting. This plant nitrosylated proteome resource expands our current understanding on NO-targeted proteins and facilitates comparisons with new nitrosylated protein data.