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(Received for publication, July 16, 1996, and in revised form, August 30, 1996)
From the Department of Biology, University of North Carolina,
Chapel Hill, North Carolina 27599-3280
The promoter of the wheat Em gene
contains elements with a CACGTG core sequence (G-boxes), which are
recognized by EmBP-1, a wheat basic/leucine zipper (bZIP) protein.
G-boxes are required for Em expression in response to the phytohormone
abscisic acid and for transactivation by the Viviparous-1 protein (VP1)
using transient expression systems. In order to identify other factors that are part of the transcriptional complex that associates with G-boxes, we have screened a rice (Oryza sativa) cDNA
library with biotinylated EmBP-1. We have isolated osZIP-1a, a homolog
of EmBP-1 and other plant G-box-binding factors. We show that EmBP-1
and osZIP-1a will preferentially heterodimerize in vitro.
Overexpression of osZIP-1a in rice protoplasts can enhance expression
from the Em promoter only in the presence of abscisic acid. Two other
clones have been identified by screening with EmBP-1: osZIP-2a and
osZIP-2b. These osZIP-2 factors represent a novel class of bZIP
proteins with an unusual DNA-binding domain that does not recognize
G-boxes. The osZIP-2 factors can heterodimerize with EmBP-1 and prevent it from binding to the Em promoter. Interestingly, osZIP-1a does not
heterodimerize with the osZIP-2 factors and its DNA binding activity is
unaffected by their presence. Thus, osZIP-2 factors may be involved in
sequestering a particular group of G-box-binding factors into inactive
heterodimers.
Volume 271, Number 49,
Issue of December 6, 1996
pp. 31296-31305
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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