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

© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 66(2015), 3 vom: 01. Feb., Seite 989-99
1. Verfasser: Holzmeister, Christian (VerfasserIn)
Weitere Verfasser: Gaupels, Frank, Geerlof, Arie, Sarioglu, Hakan, Sattler, Michael, Durner, Jörg, Lindermayr, Christian
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Antioxidant system nitric oxide nitrosative stress post-translational modification superoxide dismutase tyrosine nitration. Plant Proteins Peroxynitrous Acid 14691-52-2 mehr... Tyrosine 42HK56048U Superoxide Dismutase EC 1.15.1.1
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520 |a 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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650 4 |a nitrosative stress 
650 4 |a post-translational modification 
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650 4 |a tyrosine nitration. 
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700 1 |a Gaupels, Frank  |e verfasserin  |4 aut 
700 1 |a Geerlof, Arie  |e verfasserin  |4 aut 
700 1 |a Sarioglu, Hakan  |e verfasserin  |4 aut 
700 1 |a Sattler, Michael  |e verfasserin  |4 aut 
700 1 |a Durner, Jörg  |e verfasserin  |4 aut 
700 1 |a Lindermayr, Christian  |e verfasserin  |4 aut 
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