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J. Biol. Chem., Vol. 277, Issue 10, 7989-7995, March 8, 2002
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§,
,
, and
**
From the Previous studies have shown that the
transcriptional coactivator protein Gcn5 functions as a
catalytic histone acetyltransferase (HAT). In this work, we examine the
roles of the Ada2 and Ada3 coactivator proteins that are functionally
linked to Gcn5. We show that yeast Ada2, Ada3, and Gcn5 form a
catalytic core of the ADA and
Spt-Ada-Gcn5-acetyltransferase HAT complexes, which is necessary
and sufficient in vitro for nucleosomal HAT activity and
lysine specificity of the intact HAT complexes. We also demonstrate that Ada3 is necessary for Gcn5-dependent nucleosomal HAT
activity in yeast extracts. Our results suggest that Ada2 potentiates
the Gcn5 catalytic activity and that Ada3 facilitates nucleosomal acetylation and an expanded lysine specificity.
Center for Gene Regulation, Department of
Biochemistry and Molecular Biology, Pennsylvania State University,
University Park, Pennsylvania 16802-1014 and the ¶ Department of
Biochemistry and Molecular Genetics, University of Virginia Health
Sciences Center, Charlottesville, Virginia 22908-0733
Recipient of a Burroughs Wellcome career development award.
**
Pew Scholar in the biomedical sciences. To whom correspondence
should be addressed: Center for Gene Regulation, Dept. of Biochemistry and Molecular Biology, 108 Althouse Laboratory, Pennsylvania State University, University Park, PA 16802-1014. E-mail:
sxt30@psu.edu.
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