title: S-nitrosylation: an emerging post-translational protein modification in plants.
abstract: Increasing evidences support the assumption that nitric oxide (NO) acts as a physiological mediator in plants. Understanding its pleiotropic effects requires a deep analysis of the molecular mechanisms underlying its mode of action. In the recent years, efforts have been made in the identification of plant proteins modified by NO at the post-translational level, notably by S-nitrosylation. This reversible process involves the formation of a covalent bond between NO and reactive cysteine residues. This research has now born fruits and numerous proteins regulated by S-nitrosylation have been identified and characterized. This review describes the basic principle of S-nitrosylation as well as the Biotin Switch Technique and its recent adaptations allowing the identification of S-nitrosylated proteins in physiological contexts. The impact of S-nitrosylation on the structure/function of selected proteins is further discussed.
authors: UMR INRA 1088/CNRS 5184/Université de Bourgogne, Plante-Microbe-Environnement, F-21065 Dijon cedex, France.
authors: Jéremy
authors: J
authors: Astier
authors: Sumaira
authors: S
authors: Rasul
authors: Emmanuel
authors: E
authors: Koen
authors: Hamid
authors: H
authors: Manzoor
authors: Angélique
authors: A
authors: Besson-Bard
authors: Olivier
authors: O
authors: Lamotte
authors: Sylvain
authors: S
authors: Jeandroz
authors: Jörg
authors: J
authors: Durner
authors: Christian
authors: C
authors: Lindermayr
authors: David
authors: D
authors: Wendehenne
mesh_terms: D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D010940:Plant Proteins; D009569:Nitric Oxide