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Nitric oxide-based protein modification: Formation and site-specificity of protein S-nitrosylation.

Front. Plant Sci. 4:137 (2013)
Verlagsversion Volltext DOI
Open Access Gold
Creative Commons Lizenzvertrag
Nitric oxide (NO) is a reactive free radical with pleiotropic functions that participates in diverse biological processes in plants, such as germination, root development, stomatal closing, abiotic stress, and defense responses. It acts mainly through redox-based modification of cysteine residue(s) of target proteins, called protein S-nitrosylation.In this way NO regulates numerous cellular functions and signaling events in plants. Identification of S-nitrosylated substrates and their exact target cysteine residue(s) is very important to reveal the molecular mechanisms and regulatory roles of S-nitrosylation. In addition to the necessity of protein-protein interaction for trans-nitrosylation and denitrosylation reactions, the cellular redox environment and cysteine thiol micro-environment have been proposed important factors for the specificity of protein S-nitrosylation. Several methods have recently been developed for the proteomic identification of target proteins. However, the specificity of NO-based cysteine modification is still less defined. In this review, we discuss formation and specificity of S-nitrosylation. Special focus will be on potential S-nitrosylation motifs, site-specific proteomic analyses, computational predictions using different algorithms, and on structural analysis of cysteine S-nitrosylation.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Protein S-nitrosylation; Nitric oxide; Post-translational modification; Cysteine residue; Redox-modification; Site-specificity; Biotin-switch Assay; Dinitrosyl Iron Complexes; Nitrosated Proteins; Posttranslational Modification; Nitrosothiol Formation; Arabidopsis-thaliana; Proteomic Analysis; Endothelial-cells; Hydrogen-peroxide; Oxidative Stress
ISSN (print) / ISBN 1664-462X
e-ISSN 1664-462X
Quellenangaben Band: 4, Heft: , Seiten: , Artikelnummer: 137 Supplement: ,
Verlag Frontiers
Begutachtungsstatus Peer reviewed