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J. Biol. Chem., Vol. 276, Issue 26, 23881-23887, June 29, 2001
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From the Department of Biochemistry, Division of Nucleic Acids
Enzymology, Robert Wood Johnson Medical School, Piscataway, New Jersey
08854-5635
The bacterial
A Gal4-
54 Hybrid Protein That Functions
as a Potent Activator of RNA Polymerase II Transcription in Yeast*
,§, and
54 protein
associates with core RNA polymerase to form a holoenzyme complex that
renders cognate promoters enhancer-dependent. Although
unusual in bacteria, enhancer-dependent transcription is
the paradigm in eukaryotes. Here we report that a fragment of
Escherichia coli 54 encompassing amino acid
residues 29-177 functions as a potent transcriptional activator in
yeast when fused to a Gal4 DNA binding domain. Activation by
Gal4-54 is TATA-dependent and requires the
SAGA coactivator complex, suggesting that Gal4-54
functions by a normal mechanism of transcriptional activation. Surprisingly, deletion of the AHC1 gene, which encodes a
polypeptide unique to the ADA coactivator complex, stimulates
Gal4-54-mediated activation and enhances the toxicity of
Gal4-54. Accordingly, the SAGA and ADA complexes, both
of which include Gcn5 as their histone acetyltransferase subunit, exert
opposite effects on transcriptional activation by
Gal4-54. Gal4-54 activation and toxicity
are also dependent upon specific 54 residues that are
required for activator-responsive promoter melting by 54
in bacteria, implying that activation is a consequence of
54-specific features rather than a structurally
fortuitous polypeptide fragment. As such, Gal4-54
represents a novel tool with the potential to provide insight into the
mechanism by which natural activators function in eukaryotic cells.
*
This work was supported by National Institutes of Health
Grant GM39484 (to M. H.).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.
These two authors contributed equally to this work and should be
considered co-first authors.
§
Present address: Dept. of Biochemistry and Molecular Genetics,
University of Virginia, Charlottesville, VA 22908.
¶
To whom correspondence should be addressed: Dept. of
Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane,
Piscataway, NJ 08854-5635. Tel.: 732-235-5888; Fax: 732-235-5889;
E-mail: hampsemi@umdnj.edu.
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