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J Biol Chem, Vol. 275, Issue 17, 12879-12888, April 28, 2000
From the Vimentin is a component of the eukaryotic
cytoskeleton belonging to the family of intermediate filament proteins.
It exhibits a complex pattern of tissue- and development-specific
expression. It is also a marker of the metastatic potential of many
tumor cells. Previously, the human vimentin promoter was shown to
contain several regions for the binding of positive and negative acting regulatory factors. Until now, the silencer element, which shuts down
vimentin synthesis in selected tissues during development, was not
precisely localized; nor was its binding protein known. In
vivo DMS footprinting by ligation-mediated PCR delineated the position of guanine residues important to vimentin expression. Transient transfection assays in HeLa cells of various vimentin 5'-end
promoter sequences and mutants thereof precisely defined two regulatory
elements, a negative element and an adjoining positive acting element.
Band shift assays, UV cross-linking, and Southwestern blot analysis
confirm that the silencer element specifically binds a protein. Several
lines of evidence show that ZBP-89, a zinc finger, Kruppel-like
repressor protein is vimentin's silencer element binding factor.
Co-immunoprecipitation and DNA affinity chromatography prove that Sp1
heterodimerizes with ZBP-89 when bound to the silencer element to yield
a DNA-protein complex whose mobility is indistinguishable from that
displayed by HeLa nuclear extract in band shift assays.
The Zinc Finger Repressor, ZBP-89, Binds to the Silencer
Element of the Human Vimentin Gene and Complexes with the
Transcriptional Activator, Sp1*
§,,,
,**, and
Department of Biochemistry and Molecular
Biophysics and the Massey Cancer Center, Medical College of Virginia
Campus/Virginia Commonwealth University, Richmond, Virginia 23298 and
the ¶ Departments of Internal Medicine and Physiology and
Howard Hughes Medical Institute, University of Michigan,
Ann Arbor, Michigan 48109
*
This work was supported by NHLBI, National Institutes of
Health (NIH), Grant HL-45422 (to Z. E. Z.) and by NIDDK, NIH, Grant DK-45729 (to J. L. M.).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.
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biophysics, P.O. Box 980614, Virginia
Commonwealth University, Richmond, VA 23298. Tel.: 804-828-8753; Fax:
804-828-1473; E-mail: Zehner@hsc.vcu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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