Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
Volume 1779, Issue 10, Pages 583-589Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagrm.2008.05.007
Keywords
Basic/leucine-zipper domain; bZIP; Dimerization; NPR1; TGA factor; TGA2
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Funding
- National Science Foundation [MCB-0404746]
- University of Maryland
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Systemic acquired resistance (SAR) is triggered by hormone defense cues and is associated with the onset of expression of pathogenesis- related (PR) genes that encode for anti-microbial proteins in plants. In the case of PR-1, transcriptional activation involves promoter-specific recruitment of transcription factors such as TGA2 through a mechanism that may involve transient physical interaction with the NPR1 protein. This stimulus-inducible recruitment process has yet to be fully explained at the functional and mechanistic level. To investigate this question further, we initially looked to see whether NPR1 preferentially forms a complex the DNA bound or unbound fraction of TGA2. As shown here, NPR1 appears to preferentially interact the non-DNA bound fraction of TGA2. We subsequently Mutated this transcription factor to identify key in its conserved carboxyl terminal (CT) domain that mediate complex formation with NPR1. These revealed that two non-overlapping regions of the CT domain of TGA2 bind independently to The specificity and biological significance of these findings were inferred with a mutant form of NPR1 fails to activate SAR in vivo. These and other findings raise the possibility that NPR1 may transiently with the DNA unbound fraction of TGA2 to promote its recruitment to an active form on cognate promoters. Published by Elsevier B.V.
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