Nucleic Acids Research, Vol 24, Issue 9 1695-1701, Copyright © 1996 by Oxford University Press
TH Huang, T Oka, T Asai, T Okada, BW Merrills, PN Gertson, RH Whitson and K Itakura
We detected a novel nuclear protein, MRF, that binds to multiple sites on
the modulator which is located upstream of the human cytomegalovirus major
immediate early gene enhancer. The expression of MRF is differentiation
specific; the DNA binding activity is present in nuclear extracts from
undifferentiated Tera-2 and THP-1 cells, but significantly reduced after
these cells are induced to differentiate. In undifferentiated cells the
enhancer activity is repressed by the modulator and upon differentiation
the enhancer becomes active. Competitive binding assays demonstrate that
MRF requires the presence of multiple A+T stretches for binding to DNA,
rather than binding to a specific DNA sequence. Mutations of these
stretches in the modulator reduce the binding activity of MRF, as well as
the repressing activity on the enhancer. These results suggest that MRF may
act as a repressor of enhancer function. We propose that MRF binds over the
entire modulator and exerts repressor activity.
ARTICLES
Repression by a differentiation-specific factor of the human cytomegalovirus enhancer
Department of Molecular Genetics, Beckman Research Institute of the City of Hope, Duarte, CA 91010, USA.
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