Recruitment of HAT Complexes by Direct Activator Interactions with the ATM-Related Tra1 Subunit
Top Cited Papers
- 22 June 2001
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 292 (5525) , 2333-2337
- https://doi.org/10.1126/science.1060214
Abstract
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.Keywords
This publication has 29 references indexed in Scilit:
- Molecular Cloning and Mapping of the Brain-Abundant B1γ Subunit of Protein Phosphatase 2A, PPP2R2C, to Human Chromosome 4p16Genomics, 2000
- Mapping Protein−Protein Interactions in the Bacteriophage T4 DNA Polymerase Holoenzyme Using a Novel Trifunctional Photo-cross-linking and Affinity ReagentJournal of the American Chemical Society, 2000
- Identification and Analysis of Yeast Nucleosomal Histone Acetyltransferase ComplexesMethods, 1998
- ALTERATION OF NUCLEOSOME STRUCTURE AS A MECHANISM OF TRANSCRIPTIONAL REGULATIONAnnual Review of Biochemistry, 1998
- Induced α Helix in the VP16 Activation Domain upon Binding to a Human TAFScience, 1997
- Structural and Functional Analysis of Yeast Putative AdaptorsPublished by Elsevier ,1996
- Characterization of Physical Interactions of the Putative Transcriptional Adaptor, ADA2, with Acidic Activation Domains and TATA-binding ProteinPublished by Elsevier ,1995
- Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIBCell, 1993
- Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domainsCell, 1992
- Selective inhibition of activated but not basal transcription by the acidic activation domain of VP16: Evidence for transcriptional adaptorsCell, 1990