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Holzmeister, C. ; Gaupels, F. ; Geerlof, A. ; Sarioglu, H. ; Sattler, M. ; Durner, J. ; Lindermayr, C.

Differential inhibition of Arabidopsis superoxide dismutases by peroxynitrite-mediated tyrosine nitration.

J. Exp. Bot. 66, 989-999 (2015)
Postprint DOI PMC
Open Access Green
Despite the importance of superoxide dismutases (SODs) in the plant antioxidant defence system little is known about their regulation by post-translational modifications. Here, we investigated the in vitro effects of nitric oxide derivatives on the seven SOD isoforms of Arabidopsis thaliana. S-nitrosoglutathione, which causes S-nitrosylation of cysteine residues, did not influence SOD activities. By contrast, peroxynitrite inhibited the mitochondrial manganese SOD1 (MSD1), peroxisomal copper/zinc SOD3 (CSD3), and chloroplastic iron SOD3 (FSD3), but no other SODs. MSD1 was inhibited by up to 90% but CSD3 and FSD3 only by a maximum of 30%. Down-regulation of these SOD isoforms correlated with tyrosine (Tyr) nitration and both could be prevented by the peroxynitrite scavenger urate. Site-directed mutagenesis revealed that-amongst the 10 Tyr residues present in MSD1-Tyr63 was the main target responsible for nitration and inactivation of the enzyme. Tyr63 is located nearby the active centre at a distance of only 5.26 Å indicating that nitration could affect accessibility of the substrate binding pocket. The corresponding Tyr34 of human manganese SOD is also nitrated, suggesting that this might be an evolutionarily conserved mechanism for regulation of manganese SODs.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Antioxidant System ; Nitric Oxide ; Nitrosative Stress ; Post-translational Modification ; Superoxide Dismutase ; Tyrosine Nitration.; Protein S-nitrosylation; Nitric-oxide; Cell-death; Inactivation; Pathophysiology; Identification; Biochemistry; Defense; Residue; Rice
ISSN (print) / ISBN 0022-0957
e-ISSN 1460-2431
Journal Journal of Experimental Botany
Quellenangaben Volume: 66, Issue: 3, Pages: 989-999 Article Number: , Supplement: ,
Publisher Oxford University Press
Publishing Place Oxford
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Biochemical Plant Pathology (BIOP)
Institute of Structural Biology (STB)
CF Metabolomics & Proteomics (CF-MPC)