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J. Biol. Chem., Vol. 275, Issue 51, 40169-40173, December 22, 2000
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From the Department of Biochemistry and Molecular Genetics, School
of Medicine, University of Virginia, Charlottesville, Virginia
22908
The BRCA1 C-terminal (BRCT) domain is present in
a number of proteins that are involved in various aspects of
chromosomal events. The BRCT domain of BRCA1 is important for
its function in DNA repair and transcriptional activation. When
tethered to chromosomal DNA, this region of BRCA1 is capable of
inducing changes in chromatin structure. Despite the sequence homology
and functional proximity shared by the BRCT-containing proteins, it is
not clear whether different BRCT domains confer a common biochemical
activity. Much less is known about the functional significance of the
characteristic amino acid residues in the BRCT motif. Here, we show
that chromatin remodeling and transcription activation is not a common
feature of BRCT domains. However, the BRCT domain of the
multi-functional repressor-activator protein 1 (RAP1) can activate
transcription and remodel chromatin in a manner similar to that shown
for the BRCA1 BRCT domain. Most of the conserved amino acid residues in the second BRCA1 BRCT domain are essential for its function in transcriptional activation. In contrast, mutations of many analogous amino acid residues in the RAP1 BRCT domain greatly elevate the transcriptional activity. These data indicate that the conserved residues in these two BRCT domains may play different roles in transcriptional activation.
A Functional Comparison of BRCA1 C-terminal Domains in
Transcription Activation and Chromatin Remodeling*
*
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.
Supported by National Institutes of Health Grants RO1GM57893 and
R21CA83990 and a grant from the American Cancer Society
(RPG99-211-01-MBC). To whom correspondence should be addressed. Tel.:
804-243-2727; Fax: 804-924-5069; E-mail: rl2t@virginia.edu.
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