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J. Biol. Chem., Vol. 277, Issue 48, 46043-46050, November 29, 2002
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From the Department of Biological Chemistry and Molecular
Pharmacology, Harvard Medical School, Boston, Massachusetts 02115
Transcriptional activator proteins recruit the
RNA polymerase II machinery and chromatin-modifying activities to
promoters. Biochemical experiments indicate that activator proteins can
associate with a large number of proteins, and many such proteins have
been proposed to be direct targets of activators. However, there is great uncertainty about which biochemical interactions are
physiologically relevant. Here, we develop a formaldehyde-based
cross-linking procedure to identify protein-protein interactions that
occur under physiological conditions. We show that the VP16 activation domain directly interacts with TATA-binding protein (TBP), TFIIB, and
the SAGA histone acetylase complex in
vivo.
To whom correspondence should be addressed. Tel.: 617-432-2104;
Fax: 617-432-2529; E-mail: kevin@hms.harvard.edu.
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