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Papers In Press, published online ahead of print August 14, 2000
Dept. of Pathology, Emory University School of Medicine, Atlanta, GA 30322
Corresponding Author: pwade{at}emory.edu
The nucleosomal ATPase ISWI is the catalytic subunit of several protein complexes that either organize or perturb chromatin structure in vitro. This work reports the cloning and biochemical characterization of a Xenopus ISWI homolog. Surprisingly, while we find four complex forms of ISWI in egg extracts, we find no functional homolog of NURF. One of these complexes, xACF, consists of ISWI, Acf1, and a previously uncharacterized protein of 175 kDa. Like both ACF and CHRAC, this complex organizes randomly deposited histones into a regularly spaced array. The remaining three forms include two novel ISWI complexes distinct from known ISWI complexes plus a histone-dependent ATPase complex. This comprehensive biochemical characterization of ISWI underscores the evolutionary conservation of the ACF/CHRAC family.
J. Biol. Chem, 10.1074/jbc.M006041200
Submitted on July 10, 2000
Revised on August 7, 2000
Accepted on August 14, 2000
Multiple ISWI ATPase complexes from Xenopus laevis: functional conservation of an ACF/CHRAC homolog
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