High impact information on AT5G65210

• Furthermore, site-directed mutagenesis of TGA1 Cys-260 and Cys-266 enables the interaction with NPR1 in yeast and Arabidopsis [1].
• Together, these results indicate that TGA1 relies on the oxidation state of Cys residues to mediate the interaction with NPR1 [1].
• 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 [1].
• We show that although both TGA1 and GBF1 bind to the Hex motif (TGACGTGG), this binding can be distinguished on the basis of their specific DNA-protein contacts [2].
• TGA1 and G-box binding factors: two distinct classes of Arabidopsis leucine zipper proteins compete for the G-box-like element TGACGTGG [2].

Biological context of AT5G65210

• However, TGA1 differs from members of the GBF family in the spectrum of base pair permutations flanking the ACGT sequence that are required for DNA binding [2].
• The amino acid sequence of RGA1 was 77% and 86% identical to the sequences of alpha subunits from Arabidopsis thaliana and tomato (products of GPA1 and TGA1), respectively, and 42% to 69% identical to sequences of mammalian alpha subunits [3].

Associations of AT5G65210 with chemical compounds

• This phenomenon is correlated with a reduction of TGA1 Cys residues [1].
• Here, we report that although TGA1 does not interact with NPR1 in yeast two-hybrid assays, treatment with salicylic acid induces the interaction between these proteins in Arabidopsis leaves [1].

Other interactions of AT5G65210

• TGA3 was also found to be expressed at the same level throughout the plant, whereas genes encoding TGA1 and OBF4 have relatively high RNA expression levels in root [4].
• OBF4 is more similar to the tobacco TGA1a and Arabidopsis TGA1 proteins, while OBF5 is more similar to the maize OBF3.1, wheat HBP1b and Arabidopsis aHBP1b proteins [5].

References