Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8358492 | Plant Science | 2014 | 7 Pages |
Abstract
S-nitrosylation is a nitric oxide (NO)-based post-translational modification regulating protein function and signalling. We used a combination between the biotin switch method and labelling with isotope-coded affinity tag to identify endogenously S-nitrosylated peptides in Arabidopsis thaliana proteins extracted from plantlets. The relative level of S-nitrosylation in the identified peptides was compared between unstressed and cold-stress seedlings. We thereby detected 62 endogenously nitrosylated peptides out of which 20 are over-nitrosylated following cold exposure. Taken together these data provide a new repertoire of endogenously S-nitrosylated proteins in Arabidopsis with cysteine S-nitrosylation site. Furthermore they highlight the quantitative modification of the S-nitrosylation status of specific cysteine following cold stress.
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Agricultural and Biological Sciences
Plant Science
Authors
Juliette Puyaubert, Abasse Fares, Nathalie Rézé, Jean-Benoît Peltier, Emmanuel Baudouin,