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Molecular and Cellular Biology, January 1999, p. 855-863, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Activation Domain-Specific and General Transcription
Stimulation by Native Histone Acetyltransferase Complexes
Keiko
Ikeda,1,2
David J.
Steger,1
Anton
Eberharter,1 and
Jerry
L.
Workman1,*
Howard Hughes Medical Institute and
Department of Biochemistry and Molecular Biology, The Pennsylvania
State University, University Park, Pennsylvania
16802-4500,1 and
Department of Biology,
Jichi Medical School, Minamikawachi, Kawachi, Tochigi 329-04 Japan2
Received 22 April 1998/Returned for modification 1 June
1998/Accepted 23 September 1998
Recent progress in identifying the catalytic subunits of histone
acetyltransferase (HAT) complexes has implicated histone acetylation in
the regulation of transcription. Here, we have analyzed the function of
two native yeast HAT complexes, SAGA (Spt-Ada-Gcn5 Acetyltransferase)
and NuA4 (nucleosome acetyltransferase of H4), in activating
transcription from preassembled nucleosomal array templates in vitro.
Each complex was tested for the ability to enhance transcription driven
by GAL4 derivatives containing either acidic, glutamine-rich, or
proline-rich activation domains. On nucleosomal array templates, the
SAGA complex selectively stimulates transcription driven by the VP16
acidic activation domain in an acetyl coenzyme A-dependent manner. In
contrast, the NuA4 complex facilitates transcription mediated by any of
the activation domains tested if allowed to preacetylate the
nucleosomal template, indicating a general stimulatory effect of
histone H4 acetylation. However, when the extent of acetylation by NuA4
is limited, the complex also preferentially stimulates VP16-driven
transcription. SAGA and NuA4 interact directly with the VP16 activation
domain but not with a glutamine-rich or proline-rich activation domain.
These data suggest that recruitment of the SAGA and NuA4 HAT complexes by the VP16 activation domain contributes to HAT-dependent activation. In addition, extensive H4/H2B acetylation by NuA4 leads to a general activation of transcription, which is independent of activator-NuA4 interactions.
*
Corresponding author. Mailing address: 306 Althouse
Laboratory, The Pennsylvania State University, University Park, PA
16802-4500. Phone: (814) 863-8256. Fax: (814) 863-0099. E-mail:
JLW10{at}psu.edu.
Molecular and Cellular Biology, January 1999, p. 855-863, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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