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XB-ART-10496
J Biol Chem November 10, 2000; 275 (45): 35248-55.

Multiple ISWI ATPase complexes from xenopus laevis. Functional conservation of an ACF/CHRAC homolog.

Guschin D , Geiman TM , Kikyo N , Tremethick DJ , Wolffe AP , Wade PA .


Abstract
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, whereas 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.

PubMed ID: 10942776
Article link: J Biol Chem


Species referenced: Xenopus laevis
Genes referenced: a1cf baz1a smarca5