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Astier, J.* ; Rasul, S.* ; Koen, E.* ; Manzoor, H.* ; Besson-Bard, A.* ; Lamotte, O.* ; Jeandroz, S.* ; Durner, J. ; Lindermayr, C. ; Wendehenne, D.*

S-nitrosylation: An emerging post-translational protein modification in plants.

Plant Sci. 181, 527-533 (2011)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Nitric oxide; Plant; Post-translational protein modifications; S-nitrosothiol; S-nitrosylation
ISSN (print) / ISBN 0168-9452
e-ISSN 0168-9452
Journal Plant Science
Quellenangaben Volume: 181, Issue: 5, Pages: 527-533 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed