Nucleosome sliding via TBP DNA binding in vivo.
Here, we show that a nucleosome obstructing transcription from the IFN-beta promoter slides in vivo in response to virus infection, thus exposing the previously masked TATA box and the initiation site, a requirement for transcriptional activation. Our experiments also revealed that this mode of chromatin remodeling is a two-step reaction. First, the enhanceosome recruits the SWI/SNF chromatin-remodeling complex that modifies the nucleosome to allow binding of TBP. Second, DNA bending is induced by TBP binding, and the nucleosome slides to a new position. Experiments with other DNA binding proteins demonstrated a strong correlation between the ability to bend DNA and nucleosome sliding, suggesting that the sliding is induced by the bend.
Lomvardas
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Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY 10032, USA.
Thanos
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D015500:Chloramphenicol O-Acetyltransferase / Q000235:genetics; D002843:Chromatin / Q000502:physiology / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004742:Enhancer Elements, Genetic; D006367:HeLa Cells; D006801:Humans; D016899:Interferon-beta / Q000235:genetics*; D009707:Nucleosomes / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis; D016385:TATA Box; D035181:TATA-Box Binding Protein; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000378:metabolism*; D019473:Transcription Factors, TFII / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D014162:Transfection
D002843:Chromatin; D004268:DNA-Binding Proteins; D009707:Nucleosomes; D011994:Recombinant Proteins; D035181:TATA-Box Binding Protein; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D019473:Transcription Factors, TFII; D016899:Interferon-beta; D015500:Chloramphenicol O-Acetyltransferase