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THE PLANT CELL, Vol 4, Issue 10 1309-1319, Copyright © 1992 by American Society of Plant Biologists

RESEARCH ARTICLES

TGA1 and G-Box Binding Factors: Two Distinct Classes of Arabidopsis Leucine Zipper Proteins Compete for the G-Box-Like Element TGACGTGG

U. Schindler, H. Beckmann and A. R. Cashmore
Department of Biology, Plant Science Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018

Regulatory elements containing the sequence ACGT are found in several plant promoters and are recognized by various basic/leucine zipper (bZIP) proteins. The Arabidopsis G-box binding factor 1 (GBF1), initially identified by its ability to bind to the palindromic G-box (CCACGTGG), also interacts with the TGACGT motif if this hexamer sequence is followed by either the dinucleotide GG-as found in the Hex motif of the wheat histone 3 promoter-or GT. Here we describe the isolation of an Arabidopsis bZIP protein, denoted TGA1, that also recognizes ACGT-containing sequences. 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. TGA1 primarily requires a TGACG motif and preferentially binds to those pentamers that are followed by a T residue. 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. Furthermore, TGA1 also differs from members of the GBF family in that it apparently does not form heterodimers with any member of this family.


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Copyright © 1992 by the American Society of Plant Biologists