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Science 16 October 1998: Vol. 282. no. 5388, pp. 487 - 490 DOI: 10.1126/science.282.5388.487
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Reports
Phosphorylation and Activation of 13S Condensin by Cdc2 in Vitro
Keiji Kimura,
Michiko Hirano,
Ryuji Kobayashi,
Tatsuya Hirano
*
13S condensin is a multisubunit protein complex
essential for mitotic chromosome condensation in Xenopus egg
extracts. Purified 13S condensin introduces positive
supercoils into DNA in the presence of topoisomerase I and adenosine
triphosphate in vitro. The supercoiling activity of 13S
condensin was regulated by mitosis-specific
phosphorylation. Immunodepletion, in vitro
phosphorylation, and peptide-mapping experiments indicated
that Cdc2 is likely to be the kinase that phosphorylates and activates
13S condensin. Multiple Cdc2 phosphorylation sites are clustered in the carboxyl-terminal domain of the XCAP-D2 (Xenopus chromosome-associated polypeptide D2) subunit.
These results suggest that phosphorylation of 13S
condensin by Cdc2 may trigger mitotic chromosome condensation in
vitro.
Cold Spring Harbor Laboratory, Post Office Box 100, 1 Bungtown
Road, Cold Spring Harbor, NY 11724, USA.
*
To whom correspondence should be addressed.
Read the Full Text
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