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(Received for publication, April 11, 1997, and in revised form, May 20, 1997)
From the Matrix-associated regions (MARs), AT-rich DNA
segments that have an affinity for the nuclear matrix, have been shown
to play a role in transcriptional regulation of eukaryotic genes. The present study demonstrates that a DNA element, called L2a, which has
been implicated in the transcriptional regulation of the mouse CD8a gene encoding an important T cell coreceptor, is a
MAR. Moreover, the identities of two nuclear proteins, L2a-P1 and
L2a-P2, previously shown to bind to the L2a element, have been
determined. The L2a-P1 protein found to be present in all CD8-positive
T cell lines tested is SATB1, a known MAR-binding protein. The widely
expressed L2a-P2 protein is CDP/Cux, a MAR-binding protein that has
been associated with repression of gene transcription. Interaction of
both proteins with the L2a element was studied using the missing
nucleoside approach, DNase I footprinting, and electrophoretic mobility
shift assays with wild type and mutant L2a elements. The data suggest that CDP/Cux bound to the L2a element is displaced by binding of SATB1
and the accompanying conformational change in the DNA lying between the
primary binding sites of SATB1 and CDP/Cux. We suggest that
displacement of CDP/Cux by SATB1 favors transcription of the
CD8a gene, possibly by enhancing or altering its
association with the nuclear matrix.
Volume 272, Number 29,
Issue of July 18, 1997
pp. 18440-18452
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
,
Department of Microbiology and Institute for
Cellular and Molecular Biology, University of Texas at Austin, Austin,
Texas 78712, § Cold Spring Harbor Laboratory, Cold Spring
Harbor, New York 11724, and the ¶ Department of Immunology,
Oklahoma Medical Research Foundation,
Oklahoma City, Oklahoma 73104-5097
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