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Cell. 1995 Dec 15;83(6):1011-20.

Purification and properties of an ATP-dependent nucleosome remodeling factor.

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Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4255, USA.


We report the purification of an ATP-dependent nucleosome remodeling factor (NURF) from Drosophila embryo extracts. NURF is composed of at least four polypeptides that act in concert with the GAGA transcription factor to alter chromatin structure at the hsp70 promoter. The energy requirement is attributed to an ATPase activity that is stimulated by nucleosomes but not by free DNA or histones, suggesting that NURF acts directly on a nucleosome to perturb its structure. This finding and the physical properties of NURF contrast sharply with the multisubunit SWI2/SNF2 complex, which has also been shown to alter nucleosomes in an ATP-dependent manner. The results suggest that two distinct systems may be involved in remodeling chromatin for transcription.

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