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. 2001 Mar;7(3):539-49.
doi: 10.1016/s1097-2765(01)00201-5.

A positioned nucleosome on the human U6 promoter allows recruitment of SNAPc by the Oct-1 POU domain

X Zhao  1 , P S Pendergrast, N Hernandez
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Free article

A positioned nucleosome on the human U6 promoter allows recruitment of SNAPc by the Oct-1 POU domain

X Zhao et al. Mol Cell. 2001 Mar.
Free article

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.

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