Protein S-nitrosylation under abiotic stress : Role and mechanism

Copyright © 2024 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 207(2024) vom: 01. Feb., Seite 108329
1. Verfasser: Wang, Tong (VerfasserIn)
Weitere Verfasser: Hou, Xuemei, Wei, Lijuan, Deng, Yuzheng, Zhao, Zongxi, Liang, Chen, Liao, Weibiao
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Review Abiotic stress Nitric oxide S-nitrosoglutathione reductase S-nitrosylation Sub-cellular localization Nitric Oxide 31C4KY9ESH
Beschreibung
Zusammenfassung:Copyright © 2024 Elsevier Masson SAS. All rights reserved.
Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a redox-based posttranslational modification by covalently adding NO moiety to a reactive cysteine thiol of a target protein to form an S-nitrosothiol (SNO). Protein S-nitrosylation is an evolutionarily conserved mechanism regulating multiple aspects of cellular signaling in plant. Recently, emerging evidence have elucidated protein S-nitrosylation as a modulator of plant in responses to abiotic stress, including salt stress, extreme temperature stress, light stress, heavy metal and drought stress. In addition, significant mechanism has been made in functional characterization of protein S-nitrosylated candidates, such as changing protein conformation, and the subcellular localization of proteins, regulating protein activity and influencing protein interactions. In this study, we updated the data related to protein S-nitrosylation in plants in response to adversity and gained a deeper understanding of the functional changes of target proteins after protein S-nitrosylation
Beschreibung:Date Completed 18.03.2024
Date Revised 18.03.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2023.108329