Nucleic Acids Research, Vol 24, Issue 23 4624-4631, Copyright © 1996 by Oxford University Press
S de Pater, V Greco, K Pham, J Memelink and J Kijne
The C2-H2 zinc-finger is a widely occurring DNA binding motif, usually
present as tandem repeats. The majority of C2-H2 zinc-finger proteins that
have been studied are derived from animals. Here, we characterize a member
of a distinct class of plant C2-H2 zinc-finger proteins in detail. A cDNA
clone encoding a DNA binding protein from Arabidopsis was isolated by
SouthWestern screening. The protein, termed ZAP1 (Zinc- dependent Activator
Protein-1), is encoded by a single copy gene, which is expressed to similar
levels in root and flower, to a somewhat lower level in stem and to low
levels in leaf and siliques. The optimal binding site was determined by
random binding site selection, and the consensus sequence found is
CGTTGACCGAG. The homology between ZAP1 and other DNA binding proteins is
restricted to a repeated region of a stretch of 24 highly conserved amino
acids followed by a zinc-finger motif (C-X4-C-X22-23-H-X1-H). The
C-terminal zinc-finger region is essential for DNA binding, whereas
deletion of the N-terminal one resulted in 2.5-fold reduced binding
affinity. Binding of ZAP1 to DNA was abolished by metal-chelating agents.
The activation domain as determined in yeast is adjacent to and possibly
overlapping with the DNA binding domain. Particle bombardment experiments
with plant cells showed that ZAP1 increases expression of a gusA reporter
gene that is under control of ZAP1 binding sites. We conclude that ZAP1 is
a plant transcriptional activator with a C2-H2 zinc-finger DNA binding
domain.
ARTICLES
Characterization of a zinc-dependent transcriptional activator from Arabidopsis
Center for Phytotechnology, Leiden University, The Netherlands. sbtnbp@rulsfb.leidenuniv.nl.
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