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Originally published In Press as doi:10.1074/jbc.C000873200 on January 2, 2001

J. Biol. Chem., Vol. 276, Issue 8, 5417-5420, February 23, 2001
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ACCELERATED PUBLICATION
Chromosome Condensation by a Human Condensin Complex in Xenopus Egg Extracts*

Keiji KimuraDagger , Olivier Cuvier, and Tatsuya Hirano§

From the Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

13S condensin is a five-subunit protein complex that plays a central role in mitotic chromosome condensation. The condensin complex was originally identified and purified from Xenopus egg extracts and shown to have an ATP-dependent positive supercoiling activity in vitro. We report here the characterization of a human condensin complex purified from HeLa cell nuclear extracts. The human 13S complex has exactly the same composition as its Xenopus counterpart, being composed of two structural maintenance of chromosomes (human chromosome-associated polypeptide (hCAP)-C and hCAP-E) subunits and three non-structural maintenance of chromosomes (hCAP-D2/CNAP1, hCAP-G, and hCAP-H/BRRN) subunits. Human condensin purified from asynchronous HeLa cell cultures fails to reconfigure DNA structure in vitro. When phosphorylated by purified cdc2-cyclin B, however, it gains the ability to introduce positive supercoils into DNA in the presence of ATP and topoisomerase I. Strikingly, human condensin can induce chromosome condensation when added back into a Xenopus egg extract that has been immunodepleted of endogenous condensin. Thus, the structure and function of the condensin complex are highly conserved between Xenopus and humans, underscoring its fundamental importance in mitotic chromosome dynamics in eukaryotic cells.


* This work was supported in part by a grant from the National Institutes of Health (R01-GM53926), by the Pew Scholars Program in the Biomedical Sciences (to T. H.), by fellowships from the Leukemia and Lymphoma Society and the Robertson Research Fund (to K. K.), and by the Cold Spring Harbor Laboratory Association (to O. C.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF331796.

Dagger Present address: Cellular Physiology Laboratory, The Institute of Physical and Chemical Research (Riken), 2-1 Hirosawa, Wako, Saitama 351-01, Japan.

§ To whom correspondence should be addressed: Cold Spring Harbor Laboratory, One Bungtown Rd., P. O. Box 100, Cold Spring Harbor, NY 11724. Tel.: 516-367-8370; Fax: 516-367-8815; E-mail: hirano@cshl.org.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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