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(Received for publication, June 20, 1996, and in revised form, September 20, 1996)
From the Department of Biochemistry and Molecular Biology,
University of New Hampshire, Durham, New Hampshire 03824
The yeast transcriptional activator ADR1, which
is required for ADH2 and peroxisomal gene expression,
contains four separable and partially redundant activation domains
(TADs). Mutations in ADA2 or GCN5, encoding
components of the ADA coactivator complex involved in histone
acetylation, severely reduced LexA-ADR1-TAD activation of a
LexA-lacZ reporter gene. Similarly, the ability of the
wild-type ADR1 gene to activate an ADH2-driven
promoter was compromised in strains deleted for ADA2 or
GCN5. In contrast, defects in other general transcription
cofactors such as CCR4, CAF1/POP2, and SNF/SWI displayed much less or
no effect on LexA-ADR1-TAD activation. Using an in vitro
protein binding assay, ADA2 and GCN5 were found to specifically contact
individual ADR1 TADs. ADA2 could bind TAD II, and GCN5 physically
interacted with all four TADs. Both TADs I and IV were also shown to
make specific contacts to the C-terminal segment of TFIIB. In contrast,
no significant binding to TBP was observed. TAD IV deletion analysis
indicated that its ability to bind GCN5 and TFIIB was directly
correlated with its ability to activate transcription in
vivo. ADR1 TADs appear to make several contacts, which may help
explain both their partial redundancy and their varying requirements at
different promoters. The contact to and dependence on GCN5, a histone
acetyltransferase, suggests that rearrangement of nucleosomes may
be one important means by which ADR1 activates transcription.
Volume 271, Number 50,
Issue of December 13, 1996
pp. 32359-32365
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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