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A more recent version of this article appeared on January 1, 2002
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Submitted on September 5, 2001
Accepted on October 26, 2001
1 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York (present address: Cyclacel, Dundee Technopole, James Lindsay Place, Dundee, Scotland, United Kingdom)
2 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
3 Department of Molecular Pathology, University of Texas M.D. Anderson Cancer Center, Houston, Texas
4 Cold Spring Harbor Laboratory, One Bungtown Road, Cold Spring Harbor, New York
* Corresponding author. E-mail address: hirano{at}cshl.org.
We previously characterized major components of mitotic chromosomes assembled in Xenopus laevis egg extracts and collectively referred to them as Xenopus chromosome-associated polypeptides (XCAPs). They included five subunits of the condensin complex essential for chromosome condensation. In an effort to identify novel proteins involved in this process, we have isolated XCAP-F and found it to be the Xenopus ortholog of ISWI, a chromatin remodeling ATPase. ISWI exists in two major complexes in Xenopus egg extracts. The first complex contains ACF1 and two low-molecular-weight subunits, most likely corresponding to Xenopus CHRAC. The second complex is a novel one that contains the Xenopus ortholog of the human Williams syndrome transcription factor (WSTF). In the absence of the ISWI complexes, the deposition of histones onto DNA is apparently normal, but the spacing of nucleosomes is greatly disturbed. Despite the poor spacing of nucleosomes, ISWI depletion has little effect on DNA replication, chromosome condensation or sister chromatid cohesion in the cell-free extracts. The association of ISWI with chromatin is cell cycle-regulated, and is under the control of the INCENP-aurora B kinase complex that phosphorylates histone H3 during mitosis. Apparently contradictory to the generally accepted model, we find that neither chromosome condensation nor chromosomal targeting of condensin is compromised when H3 phosphorylation is drastically reduced by depletion of INCENP-aurora B.
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