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The coactivator function of Arabidopsis NPR1 requires the core of its BTB/POZ domain and the oxidation of C-terminal cysteines. | LitMetric

AI Article Synopsis

  • NPR1 is crucial for systemic acquired resistance (SAR) in Arabidopsis thaliana, and salicylic acid treatment causes specific cysteine residues in NPR1 to reduce, aiding in its movement into the nucleus where it activates defense genes.
  • TGA2, a transcription factor, is shown to be a transcriptional repressor on its own but can form a transactivating complex with NPR1 after salicylic acid stimulation, leading to the activation of the PR-1 gene.
  • This study highlights the role of NPR1's unique cysteine oxidation in modulating TGA2's function and enhances our understanding of how these proteins work together to regulate plant defense mechanisms.

Article Abstract

NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. The interaction of nucleus-localized NPR1 with TGA transcription factors results in the activation of defense genes, including the SAR marker PATHOGENESIS-RELATED-1 (PR-1), and the deployment of SAR. Little is known about how TGA factors or NPR1 regulate transcription or whether a TGA-NPR1 complex forms on DNA. We show that TGA2 and NPR1 are recruited to PR-1 independently of each other and of SA treatment. Consistent with the result that a triple knockout in TGA2/5/6 derepresses PR-1, in vivo plant transcription assays revealed that TGA2 is not an autonomous transcription activator but is a transcriptional repressor in both untreated and SA-treated cells. However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. These Cys residues are found in a new type of transactivation domain that we term Cys-oxidized. These data further our understanding of the mechanism by which TGA2 and NPR1 activate Arabidopsis PR-1.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1785396PMC
http://dx.doi.org/10.1105/tpc.106.046953DOI Listing

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