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Science 22 June 2001: Vol. 292. no. 5525, pp. 2333 - 2337 DOI: 10.1126/science.1060214
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Reports
Recruitment of HAT Complexes by Direct Activator Interactions with the ATM-Related Tra1 Subunit
Christine E. Brown,12
LeAnn Howe,12
Kyle Sousa,12
Stephen C. Alley,3
Michael J. Carrozza,12
Song Tan,2
Jerry L. Workman1*
Promoter-specific recruitment of histone acetyltransferase activity
is often critical for transcriptional activation. We present a detailed
study of the interaction between the histone acetyltransferase complexes SAGA and NuA4, and transcription activators. We demonstrate by affinity chromatography and photo-cross-linking label transfer that
acidic activators directly interact with Tra1p, a shared subunit of
SAGA and NuA4. Mutations within the COOH-terminus of Tra1p disrupted
its interaction with activators and resulted in gene-specific
transcriptional defects that correlated with lowered promoter-specific
histone acetylation. These data demonstrate that the essential Tra1
protein serves as a common target for activators in both SAGA and NuA4
acetyltransferases.
1 Howard Hughes Medical Institute,
2 Department of Biochemistry and Molecular Biology,
3 Department of Chemistry, The Pennsylvania State
University, 306 Althouse Laboratory, University Park, PA 16802, USA.
*
To whom correspondence should be addressed: E-mail:
jlw10{at}psu.edu
Read the Full Text
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