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A more recent version of this article appeared on February 16, 2001
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Papers In Press, published online ahead of print January 2, 2001
J. Biol. Chem, 10.1074/jbc.C000873200
Submitted on December 11, 2000
Revised on December 28, 2000
Accepted on January 2, 2001

Chromosome condensation by a human condensin complex in Xenopus egg extracts

Keiji Kimura, Olivier Cuvier, and Tatsuya Hirano

Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724

Corresponding Author: hirano{at}cshl.org

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 SMC (hCAP-C and hCAP-E) and three non-SMC (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.


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