1. A Positioned Nucleosome on the Human U6 Promoter Allows Recruitment of SNAPc by the Oct-1 POU Domain
- Author
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P. Shannon Pendergrast, Nouria Hernandez, and Xinyang Zhao
- Subjects
Transcriptional Activation ,genetic structures ,DNA Footprinting ,Molecular Conformation ,DNA footprinting ,Biology ,Response Elements ,Models, Biological ,Transcription (biology) ,RNA, Small Nuclear ,Humans ,Micrococcal Nuclease ,Nucleosome ,RNA, Messenger ,Binding site ,Promoter Regions, Genetic ,Molecular Biology ,Genetics ,POU domain ,General transcription factor ,Cooperative binding ,Promoter ,DNA ,Templates, Genetic ,Cell Biology ,Nucleosomes ,Protein Structure, Tertiary ,Cell biology ,DNA-Binding Proteins ,Host Cell Factor C1 ,Allosteric Site ,HeLa Cells ,Octamer Transcription Factor-1 ,Protein Binding ,Transcription Factors - Abstract
The human snRNA promoters contain a proximal sequence element (PSE) required for basal transcription and a distal sequence element (DSE) required for activated transcription. The PSE recruits the multisubunit factor SNAPc, whereas the DSE recruits Oct-1. Oct-1 and SNAPc bind cooperatively to DNA when their respective binding sites are moved into proximity through a mechanism that involves a defined protein-protein contact. Here, we show that on the natural U6 promoter, cooperative binding of Oct-1 and SNAPc is mediated by a positioned nucleosome that resides between the DSE and the PSE. This cooperative binding requires the same protein-protein contact as cooperative binding to closely spaced sites on naked DNA and mediates transcription activation.
- Published
- 2001
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