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Vol. 16, No. 16, pp. 2120-2134, August 15, 2002
Howard Hughes Medical Institute and the Department of Oncological
Sciences, Huntsman Cancer Institute, University of Utah School of
Medicine, Salt Lake City, Utah 84112, USA
Chromatin-remodeling complexes couple ATP hydrolysis to alterations
in histone-DNA interactions and nucleosome mobility, allowing transcription factors access to chromatin. Here, we use triple-helix strand-displacement assays, DNA length-dependent ATPase assays, and
DNA-minicircle ATPase assays to establish that RSC, as well as its
isolated ATPase subunit Sth1, are DNA translocases. RSC/Sth1 ATPase
activity is stimulated by single-stranded DNA, suggesting that Sth1
tracks along one strand of the DNA duplex. Each RSC complex appears to
contain a single molecule of Sth1, and isolated Sth1 is capable of
nucleosome remodeling. We propose that the remodeling enzyme remains in
a fixed position on the octamer and translocates a segment of DNA (with
accompanying DNA twist), which breaks histone-DNA contacts and
propagates as a wave of DNA around the octamer. The demonstration of
DNA translocation presented here provides a mechanistic basis for this
DNA wave. To test the relative contribution of twist to remodeling, we
use nucleosomes containing nicks in precise locations to uncouple twist
and translocation. Nucleosomes bearing nicks are remodeled less
efficiently than intact nucleosomes. These results suggest that RSC and
Sth1 are DNA translocases that use both DNA translocation and twist to remodel nucleosomes efficiently.
[Key Words: RSC; Sth1; chromatin; nucleosome; translocation; SWI/SNF]
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