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

Holzmeister C, Gaupels F, Geerlof A, Sarioglu H, Sattler M, Durner J, Lindermayr C - J. Exp. Bot. (2014)

Bottom Line: 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.The corresponding Tyr34 of human manganese SOD is also nitrated, suggesting that this might be an evolutionarily conserved mechanism for regulation of manganese SODs.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.

No MeSH data available.


Detection of nitrated Tyr residues. Purified, recombinant MSD1, FSD3, and Cu/ZnSOD3 were treated with different concentrations of peroxynitrite, separated by SDS-PAGE, and blotted onto nitrocellulose membrane. Detection of nitrated Tyr residues was achieved using anti-NO2–Tyr antibody. Treatment with 500 µM peroxynitrite in presence of 100 µM urate was used as control.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC4321555&req=5

Figure 5: Detection of nitrated Tyr residues. Purified, recombinant MSD1, FSD3, and Cu/ZnSOD3 were treated with different concentrations of peroxynitrite, separated by SDS-PAGE, and blotted onto nitrocellulose membrane. Detection of nitrated Tyr residues was achieved using anti-NO2–Tyr antibody. Treatment with 500 µM peroxynitrite in presence of 100 µM urate was used as control.

Mentions: Inhibition of enzyme activity by ONOO– correlated with increased protein nitration as detected by immunoblot analyses using an anti-nitrotyrosine antibody (Fig. 5). Notably, western blot signals were stronger for MSD1 than FSD3 and CSD3. Because of the high sensitivity of MSD1 to ONOO– this isoform has been analysed in more detail.


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

Holzmeister C, Gaupels F, Geerlof A, Sarioglu H, Sattler M, Durner J, Lindermayr C - J. Exp. Bot. (2014)

Detection of nitrated Tyr residues. Purified, recombinant MSD1, FSD3, and Cu/ZnSOD3 were treated with different concentrations of peroxynitrite, separated by SDS-PAGE, and blotted onto nitrocellulose membrane. Detection of nitrated Tyr residues was achieved using anti-NO2–Tyr antibody. Treatment with 500 µM peroxynitrite in presence of 100 µM urate was used as control.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4321555&req=5

Figure 5: Detection of nitrated Tyr residues. Purified, recombinant MSD1, FSD3, and Cu/ZnSOD3 were treated with different concentrations of peroxynitrite, separated by SDS-PAGE, and blotted onto nitrocellulose membrane. Detection of nitrated Tyr residues was achieved using anti-NO2–Tyr antibody. Treatment with 500 µM peroxynitrite in presence of 100 µM urate was used as control.
Mentions: Inhibition of enzyme activity by ONOO– correlated with increased protein nitration as detected by immunoblot analyses using an anti-nitrotyrosine antibody (Fig. 5). Notably, western blot signals were stronger for MSD1 than FSD3 and CSD3. Because of the high sensitivity of MSD1 to ONOO– this isoform has been analysed in more detail.

Bottom Line: 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.The corresponding Tyr34 of human manganese SOD is also nitrated, suggesting that this might be an evolutionarily conserved mechanism for regulation of manganese SODs.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemical Plant Pathology, Helmholtz Zentrum München-German Research Center for Environmental Health, 85764 München/Neuherberg, Germany.

No MeSH data available.