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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.


Structural model of Arabidopsis MSD1. The structural model of Arabidopsis MSD1 was generated using SWISS-MODEL with the crystal structure of Caenorhabditis elegans MnSOD as template (PDBcode: PDB 3DC6). The Tyr residues are marked in green. The distances between Tyr side chains and the active side manganese ion (yellow) is given in Ångström in brackets.
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Figure 6: Structural model of Arabidopsis MSD1. The structural model of Arabidopsis MSD1 was generated using SWISS-MODEL with the crystal structure of Caenorhabditis elegans MnSOD as template (PDBcode: PDB 3DC6). The Tyr residues are marked in green. The distances between Tyr side chains and the active side manganese ion (yellow) is given in Ångström in brackets.

Mentions: To identify the modified Tyr residues in MSD1, peroxynitrite-treated MSD1 was analysed by mass spectrometry. In total, MSD1 has ten Tyr residues. Modelling of the three-dimensional structure of MSD11 revealed that especially Tyr63, Tyr198, and Tyr209 were located close to an active site manganese ion at a distance lower than 10 Å (5.3 Å, 9.1 Å, 9.3 Å, respectively) (Fig. 6). MSD1 was treated with 500 µM peroxynitrite and digested with trypsin. This protease generated analysable peptides containing the different Tyr residues mentioned above. For each nitrated Tyr residue an increase in mass by 45Da was expected. All identified nitrated Tyr residues are summarized in Table 2. Tyr residues 209, 221, and 226 are not accessible to nitration, as they were only found in their unmodified form. Especially nitration of Tyr63, which is closest to the active site manganese, could be of special importance for the inhibitory effect of peroxynitrite on MSD1, as it corresponds to Tyr34 in human MnSOD.


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)

Structural model of Arabidopsis MSD1. The structural model of Arabidopsis MSD1 was generated using SWISS-MODEL with the crystal structure of Caenorhabditis elegans MnSOD as template (PDBcode: PDB 3DC6). The Tyr residues are marked in green. The distances between Tyr side chains and the active side manganese ion (yellow) is given in Ångström in brackets.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 6: Structural model of Arabidopsis MSD1. The structural model of Arabidopsis MSD1 was generated using SWISS-MODEL with the crystal structure of Caenorhabditis elegans MnSOD as template (PDBcode: PDB 3DC6). The Tyr residues are marked in green. The distances between Tyr side chains and the active side manganese ion (yellow) is given in Ångström in brackets.
Mentions: To identify the modified Tyr residues in MSD1, peroxynitrite-treated MSD1 was analysed by mass spectrometry. In total, MSD1 has ten Tyr residues. Modelling of the three-dimensional structure of MSD11 revealed that especially Tyr63, Tyr198, and Tyr209 were located close to an active site manganese ion at a distance lower than 10 Å (5.3 Å, 9.1 Å, 9.3 Å, respectively) (Fig. 6). MSD1 was treated with 500 µM peroxynitrite and digested with trypsin. This protease generated analysable peptides containing the different Tyr residues mentioned above. For each nitrated Tyr residue an increase in mass by 45Da was expected. All identified nitrated Tyr residues are summarized in Table 2. Tyr residues 209, 221, and 226 are not accessible to nitration, as they were only found in their unmodified form. Especially nitration of Tyr63, which is closest to the active site manganese, could be of special importance for the inhibitory effect of peroxynitrite on MSD1, as it corresponds to Tyr34 in human MnSOD.

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.