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J. Biol. Chem., Vol. 277, Issue 28, 25115-25124, July 12, 2002
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,
,
§, and
¶
From the Previously, we and others reported that the high
mobility group proteins, HMGB-1/-2, enhance DNA binding in
vitro and transactivation in situ by the steroid
hormone subgroup of nuclear receptors but did not influence these
functions of class II receptors. We show here that the DNA binding
domain (DBD) is sufficient to account for the selective influence of
HMGB-1/-2 on the steroid class of receptors. Furthermore, the use of
chimeric DBDs reveals that this selectivity is dependent on the
C-terminal extension (CTE), amino acid sequences adjacent to the zinc
finger core DBD. HMGB-1/-2 interact directly with the DBDs of steroid
but not class II receptors, and this interaction requires the CTE. This
in vitro interaction correlates with a requirement of the
CTE for maximal HMGB-1/-2 enhancement of DNA binding in
vitro and transcriptional activation in cells. Finally, class II
receptor DBDs have a much higher intrinsic affinity for DNA than
steroid receptor DBDs, and this affinity difference is also dependent
on the CTE. These results reveal the importance of the steroid receptor
CTE for DNA binding affinity and functional response to
HMGB-1/-2.
Program in Molecular Biology and the
Departments of § Pharmacology and ¶ Pathology,
University of Colorado Health Sciences Center,
Denver, Colorado 80262
To whom correspondence should be addressed: Dept. of
Pathology, University of Colorado Health Sciences Center, 4200 E. Ninth Ave., B216, Denver, CO 80262. Tel.: 303-315-5416; Fax: 303-315-6721; E-mail: dean.edwards@uchsc.edu.
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