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J Biol Chem, Vol. 275, Issue 16, 11799-11808, April 21, 2000
From the To investigate the transcriptional mechanisms of
rice tungro bacilliform virus, we have systematically analyzed an
activator element located immediately upstream of the TATA box in the
rice tungro bacilliform virus promoter and its cognate
trans-acting factors. Using electrophoretic mobility shift
assays, we showed that rice nuclear proteins bind to the activator
element, forming multiple specific DNA-protein complexes via
protein-protein interactions. Copper-phenanthroline footprinting and
DNA methylation interference analysis indicated that multiple
DNA-protein complexes share a common binding site located between
positions
Transcriptional Activation of the Rice Tungro Bacilliform Virus
Gene Is Critically Dependent on an Activator Element Located
Immediately Upstream of the TATA Box*
,§, and Friedrich Miescher Institute, P. O. Box
2543, CH-4002 Basel and the ¶ Institute of Plant Sciences,
Federal Institute of Technology, Zürich,
Zürich CH-8092, Switzerland
60 to 39, and the proteins contact the activator element
in the major groove. DNA UV cross-linking assays further showed that
two nuclear proteins (36 and 33 kDa), found in rice cell suspension and
shoot nuclear extracts, and one (27 kDa), present in root nuclear
extracts, bind to this activator element. In protoplasts derived from a rice (Oryza sativa) suspension culture, the activator
element is a prerequisite for promoter activity and its function is
critically dependent on its position relative to the TATA box. Thus,
transcriptional activation may function via interactions with the basal
transcriptional machinery, and we propose that this activation is
mediated by protein-protein interactions in a
position-dependent mechanism.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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