Abstract
The Epstein-Barr virus nuclear antigen 2 (EBNA-2) acidic domain is essential for B-lymphocyte growth transformation and can activate transcription when brought to a promoter by a sequence-specific DNA-binding domain. We now show that the EBNA-2 acidic domain has slightly less activity than the proteotypic acidic transactivator VP16 in depleting nuclear extracts of basal transcription activity. Like VP16, EBNA-2 associates with TFIIB, TAF40, and RPA70. However, EBNA-2 has much less avidity for TATA-binding protein. A Trp-to-Thr mutation within the acidic domain abolishes EBNA-2 transactivating activity and greatly compromises the association with TFIIB, TAF40, and RPA70, establishing a genetic linkage between transactivating activity and these associations.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antigens, Viral / chemistry
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Antigens, Viral / metabolism*
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Base Sequence
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DNA Primers
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism*
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Drosophila Proteins*
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Epstein-Barr Virus Nuclear Antigens
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Hydrogen-Ion Concentration
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Molecular Sequence Data
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Replication Protein A
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TATA Box*
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TATA-Binding Protein Associated Factors*
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TATA-Box Binding Protein
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Trans-Activators / metabolism
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Transcription Factor TFIIB
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Transcription Factor TFIID*
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Transcription Factors / metabolism*
Substances
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Antigens, Viral
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DNA Primers
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DNA-Binding Proteins
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Drosophila Proteins
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Epstein-Barr Virus Nuclear Antigens
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Replication Protein A
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TATA-Binding Protein Associated Factors
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TATA-Box Binding Protein
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Trans-Activators
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Transcription Factor TFIIB
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Transcription Factor TFIID
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Transcription Factors
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e(y)1 protein, Drosophila