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The BTB/POZ Domain of the Arabidopsis Disease Resistance Protein NPR1 Interacts with the Repression Domain of TGA2 to Negate Its Function 总被引:1,自引:0,他引:1
Patrick Boyle Errol Le Su Amanda Rochon Heather L. Shearer Jhadeswar Murmu Jee Yan Chu Pierre R. Fobert Charles Després 《The Plant cell》2009,21(11):3700-3713
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The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domain/leucine zipper transcription factor TGA1 总被引:12,自引:0,他引:12
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Després C Chubak C Rochon A Clark R Bethune T Desveaux D Fobert PR 《The Plant cell》2003,15(9):2181-2191
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Zhou JM Trifa Y Silva H Pontier D Lam E Shah J Klessig DF 《Molecular plant-microbe interactions : MPMI》2000,13(2):191-202
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Redox control of systemic acquired resistance 总被引:1,自引:0,他引:1
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Weigel Ralf R. Bäuscher Christoph Pfitzner Artur J.P. Pfitzner Ursula M. 《Plant molecular biology》2001,46(2):143-160
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Christian Lindermayr Simone Sell Bernd Müller Dario Leister J?rg Durner 《The Plant cell》2010,22(8):2894-2907
The role of reactive oxygen and nitrogen species in local and systemic defense reactions is well documented. NPR1 and TGA1 are key redox-controlled regulators of systemic acquired resistance in plants. NPR1 monomers interact with the reduced form of TGA1, which targets the activation sequence-1 (as-1) element of the promoter region of defense proteins. Here, we report the effect of the physiological nitric oxide donor S-nitrosoglutathione on the NPR1/TGA1 regulation system in Arabidopsis thaliana. Using the biotin switch method, we demonstrate that both NPR1 and TGA1 are S-nitrosylated after treatment with S-nitrosoglutathione. Mass spectrometry analyses revealed that the Cys residues 260 and 266 of TGA1 are S-nitrosylated and S-glutathionylated even at GSNO concentrations in the low micromolar range. Furthermore, we showed that S-nitrosoglutathione protects TGA1 from oxygen-mediated modifications and enhances the DNA binding activity of TGA1 to the as-1 element in the presence of NPR1. In addition, we observed that the translocation of NPR1 into the nucleus is promoted by nitric oxide. Taken together, our results suggest that nitric oxide is a redox regulator of the NPR1/TGA1 system and that they underline the importance of nitric oxide in the plant defense response. 相似文献
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