Abstract
We have identified a conserved region in the C-terminal domain of bromodomain-containing protein 4 (BRD4) that mediates its specific interaction with positive transcription elongation factor b (P-TEFb). This domain is highly conserved in testis-specific bromodomain protein (BRDT) and Drosophila fs(1)h. Both BRDT and fs(1)h specifically interact with P-TEFb in mammalian cells, and this interaction depends on their C-terminal domains. Overexpression of the BRD4 P-TEFb-interacting domain disrupts the interaction between the HIV transactivator Tat and P-TEFb and suppresses the ability of Tat to transactivate the HIV promoter. Incubation of cells with a synthetic peptide containing the C-terminal domain of BRD4 interferes with transactivation of the HIV promoter by the Tat protein.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Cycle Proteins
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Cell Line
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Conserved Sequence
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Gene Products, tat / genetics
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Gene Products, tat / metabolism
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HIV / genetics*
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Humans
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Positive Transcriptional Elongation Factor B / genetics
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Positive Transcriptional Elongation Factor B / metabolism*
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Promoter Regions, Genetic / genetics
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Protein Binding
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Protein Subunits / genetics
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Protein Subunits / metabolism
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Sequence Alignment
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription, Genetic / genetics*
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Transcriptional Activation / genetics
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tat Gene Products, Human Immunodeficiency Virus
Substances
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BRD4 protein, human
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Cell Cycle Proteins
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Gene Products, tat
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Nuclear Proteins
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Protein Subunits
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Transcription Factors
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tat Gene Products, Human Immunodeficiency Virus
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Positive Transcriptional Elongation Factor B