GSNOR-mediated de-nitrosylation in the plant defence response

Crown Copyright © 2011. Published by Elsevier Ireland Ltd. All rights reserved.

Détails bibliographiques
Publié dans:Plant science : an international journal of experimental plant biology. - 1985. - 181(2011), 5 vom: 15. Nov., Seite 540-4
Auteur principal: Malik, Saad I (Auteur)
Autres auteurs: Hussain, Adil, Yun, Byung-Wook, Spoel, Steven H, Loake, Gary J
Format: Article en ligne
Langue:English
Publié: 2011
Accès à la collection:Plant science : an international journal of experimental plant biology
Sujets:Journal Article Research Support, Non-U.S. Gov't Review S-Nitrosothiols Nitric Oxide 31C4KY9ESH Aldehyde Oxidoreductases EC 1.2.- formaldehyde dehydrogenase, glutathione-independent EC 1.2.1.46 plus... Salicylic Acid O414PZ4LPZ
Description
Résumé:Crown Copyright © 2011. Published by Elsevier Ireland Ltd. All rights reserved.
A key feature of the plant defence response is the transient engagement of a nitrosative burst, resulting in the synthesis of reactive nitrogen intermediates (RNIs). Specific, highly reactive cysteine (Cys) residues of low pK(a) are a major site of action for these intermediates. The addition of an NO moiety to a Cys thiol to form an S-nitrosothiol (SNO), is termed S-nitrosylation. This redox-based post-translational modification is emerging as a key regulator of protein function in plant immunity. Here we highlight recent advances in our understanding of de-nitrosylation, the mechanism that depletes protein SNOs, with a focus on S-nitrosoglutathione reductase (GSNOR). This enzyme controls total cellular S-nitrosylation indirectly during the defence response by turning over S-nitrosoglutathione (GSNO), a major cache of NO bioactivity
Description:Date Completed 20.12.2011
Date Revised 16.03.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2011.04.004