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THE PLANT CELL, Vol 6, Issue 12 1805-1813, Copyright © 1994 by American Society of Plant Biologists
Molecular Dissection of GT-1 from Arabidopsis
K. Hiratsuka, X. Wu, H. Fukuzawa and N. H. Chua
Laboratory of Plant Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10021-6399
We isolated and characterized an Arabidopsis cDNA encoding the DNA binding
protein GT-1. This protein factor, which contains 406 amino acids, is
highly homologous to the previously described tobacco DNA binding protein
GT-1a/B2F but is 26 amino acids longer. Recombinant Arabidopsis GT-1, which
was obtained from in vitro translation, bound to probes consisting of four
copies of pea small subunit of ribulose bisphosphate carboxylase rbcS-3A
box II and required the same GGTTAA core binding site as the binding
activity of an Arabidopsis nuclear protein preparation. However, unlike the
truncated tobacco GT-1a prepared from Escherichia coli extracts, the
full-length Arabidopsis GT-1 bound to pea rbcS-3A box III and Arabidopsis
chlorophyll a/b binding protein CAB2 light-responsive elements, both of
which contain GATA motifs. Deletion and mutational analyses suggested that
the predicted trihelix region of GT-1 is essential for DNA binding.
Moreover, GT-1 binds to target DNA as a dimer, and its C-terminal region
contains a putative dimerization domain that enhances the binding activity.
Transient expression of the GT-1::[beta]-glucuronidase fusion protein in
onion cells revealed the presence of a nuclear localization signal(s)
within the first 215 amino acids of GT-1.
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