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. 2014 Mar 4;2(1):85–106. doi: 10.3390/proteomes2010085

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© 2014 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Two distinct mechanisms of basic leucine zipper containing domain proteins (bZIP) protein actions during plant defense responses. (A) The attack of a biotrophic pathogen triggers a signaling pathway mediated by salicylic acid resulting in the dissociation of the non-expresser of pathogen-related (PR) (NPR1) protein, which translocates to the nucleus and activates the expression of SA-responsive genes by interaction with the TGACGTCA cis-element-binding protein (TGA) bZIP trans-acting factors. The NPR1 protein is ubiquitinated and targeted for degradation by the 26S proteasome complex; (B) Recognition of elicitors after pathogen attack promotes the dissociation of the BZI1/ANK1 and AtbZIP10/LSD1 complexes, favoring the positive transcriptional regulation of hypersensitive response (HR)- and basal defense-related genes.