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XB-ART-14127
Science 1998 Oct 16;2825388:487-90. doi: 10.1126/science.282.5388.487.
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Phosphorylation and activation of 13S condensin by Cdc2 in vitro.

Kimura K , Hirano M , Kobayashi R , Hirano T .


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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 13Scondensin 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 13Scondensin by Cdc2 may trigger mitotic chromosome condensation in vitro.

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Species referenced: Xenopus
Genes referenced: cdk1 pold1

References :
Murray, How to compact DNA. 1998, Pubmed, Xenbase