Multiple ISWI ATPase complexes from Xenopus laevis: Functional conservation of an ACF/CHRAC homolog

Dmitry Guschin, Theresa M. Geiman, Nobuaki Kikyo, David J. Tremethick, Alan P. Wolffe, Paul A. Wade

Research output: Contribution to journalArticlepeer-review

62 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)35248-35255
Number of pages8
JournalJournal of Biological Chemistry
Volume275
Issue number45
DOIs
StatePublished - Nov 10 2000

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