Phosphorylation and Activation of 13 S Condensin by Cdc2 in Vitro

13 S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 13 S condensin introduces positive supercoils into DNA in the presence of topoisomerase I and adenosine triphosphate in vitro. The supercoiling activity of 13 S condensin...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1998-10, Vol.282 (5388), p.487-490
Hauptverfasser: Kimura, Keiji, Hirano, Michiko, Kobayashi, Ryuji, Hirano, Tatsuya
Format: Artikel
Sprache:eng
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Zusammenfassung:13 S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 13 S condensin introduces positive supercoils into DNA in the presence of topoisomerase I and adenosine triphosphate in vitro. The supercoiling activity of 13 S 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 13 S 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 13 S condensin by Cdc2 may trigger mitotic chromosome condensation in vitro.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.282.5388.487