Abstract
Protein–protein interactions are important for the molecular understanding of the biological processes of proteins. The dimerization of bZIPs (basic leucine zipper proteins) is involved in modifying binding site specificities, altering dimer stability, and permitting a new set of specific protein-to-protein interactions to occur at the promoter. In the present study, we studied the whether ThbZIP1 form homo- and heterodimers using the yeast two-hybrid method. Five bZIP genes were cloned from Tamarix hispida to investigate their interaction with ThbZIP1. Our results showed that ThbZIP1 can form homodimers with itself, and three out of five bZIPs could interact with the ThbZIP1 protein to form heterodimers. Real-time RT-PCR results suggested that these ThbZIPs can all respond to abiotic stresses and abscisic acid (ABA), and shared very similar expression patterns in response to NaCl, ABA or PEG6000. Subcellular localization studies showed that all ThbZIPs are targeted to the nucleus. Our results showed that ThbZIP1 are dimeric proteins, which can form homo- or heterodimers.
Highlights
Basic leucine zipper proteins are a large family of transcription factors (TFs) in plants, basic leucine zipper (bZIP) TFs contain a characteristic and highly conserved basic domain with two structural features: the basic/positively charged sequence, which serves as both a DNA binding and nuclear localization element, and a leucine zipper dimerization element [1,2]
The expression of ThbZIP1 is induced by abscisic acid (ABA), salt and drought
The Arabidopsis plant that overexpressed ThbZIP1 had an increased tolerance to drought and salt compared with wild-type (Col-0) Arabidopsis
Summary
Basic leucine zipper proteins (bZIPs) are a large family of transcription factors (TFs) in plants, bZIP TFs contain a characteristic and highly conserved basic domain with two structural features: the basic/positively charged sequence, which serves as both a DNA binding and nuclear localization element, and a leucine zipper dimerization element [1,2]. Heterodimerization in yeast has been confirmed in vitro by EMSA (electrophoretic mobility shift assay) studies and in plants using a protoplast two-hybrid system [7]. TFs of the bZIP family bind to DNA predominantly as homo- or heterodimers [4,12,13]. Three tobacco bZIP heterodimerization partners have been isolated which form specific heterodimers with BZI-1, namely BZI-2, BZI-3, and BZI-4 (bZIP TFs) [15]. They provide in vivo evidence that ProDH is not regulated by a single bZIP, but by a complex heterodimerization network of group-S1/C bZIP factors [17]. The efficiency of the system was tested by examining the homo- and heterodimerization properties of basic leucine zipper (bZIP) transcription factors. We investigated whether ThbZIP1 could homo- or heterodimerize by the yeast two-hybrid system
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