Abstract
We have asked how the human cytomegalovirus major immediate-early 1 (IE1) and 2 (IE2) proteins act to transactivate heterologous cellular and viral promoters. Here we show that transactivation of the human immunodeficiency virus long terminal repeat and the 70,000-molecular-weight heat shock protein (hsp70) promoter by IE1 is TATA box independent and that the IE1 protein does not interact directly with the TATA box-binding factor TFIID. Conversely, transactivation of these promoters by IE2 is TATA box dependent and a direct interaction between IE2 and TFIID occurs, suggesting that IE2 transactivation is mediated through interaction with TFIID.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cells, Cultured
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Cytomegalovirus / genetics*
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HIV Long Terminal Repeat
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HIV-1 / genetics*
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Heat-Shock Proteins / genetics
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Immediate-Early Proteins / metabolism*
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Membrane Glycoproteins*
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Promoter Regions, Genetic*
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Repetitive Sequences, Nucleic Acid / genetics
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TATA Box*
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Trans-Activators*
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Transcription Factor TFIID
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Transcription Factors / metabolism*
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Transcriptional Activation*
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Viral Envelope Proteins*
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Viral Proteins*
Substances
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Heat-Shock Proteins
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IE1 protein, cytomegalovirus
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IE2 protein, Cytomegalovirus
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Immediate-Early Proteins
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Membrane Glycoproteins
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Trans-Activators
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Transcription Factor TFIID
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Transcription Factors
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UL115 protein, Human herpesvirus 5
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Viral Envelope Proteins
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Viral Proteins
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glycoprotein H, Cytomegalovirus
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glycoprotein H, Human cytomegalovirus
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glycoprotein O, cytomegalovirus