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J. Biol. Chem., Vol. 275, Issue 45, 35248-35255, November 10, 2000
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From the 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.
Multiple ISWI ATPase Complexes from Xenopus
laevis
FUNCTIONAL CONSERVATION OF AN ACF/CHRAC HOMOLOG*
§,¶,¶,
,§, and**
Laboratory of Molecular Embryology, NICHD,
National Institutes of Health, Bethesda, Maryland 20892 and
John Curtin School of Medical Research, The Australian National
University, Canberra, ACT 2601, Australia
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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