Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit.
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.
Mesh Terms:
Acetylation, Acetyltransferases, Alleles, CCAAT-Binding Factor, Cross-Linking Reagents, DNA-Binding Proteins, Fungal Proteins, Histone Acetyltransferases, Histones, Mutation, Promoter Regions, Genetic, Protein Kinases, Protein Subunits, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae Proteins, TATA-Binding Protein Associated Factors, Temperature, Trans-Activators, Transcription Factor TFIID, Transcription Factors, Transcriptional Activation, Yeasts
Acetylation, Acetyltransferases, Alleles, CCAAT-Binding Factor, Cross-Linking Reagents, DNA-Binding Proteins, Fungal Proteins, Histone Acetyltransferases, Histones, Mutation, Promoter Regions, Genetic, Protein Kinases, Protein Subunits, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae Proteins, TATA-Binding Protein Associated Factors, Temperature, Trans-Activators, Transcription Factor TFIID, Transcription Factors, Transcriptional Activation, Yeasts
Science
Date: Jun. 22, 2001
PubMed ID: 11423663
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