Phosphorylation and activation of 13S condensin by Cdc2 in vitro

被引:249
作者
Kimura, K [1 ]
Hirano, M [1 ]
Kobayashi, R [1 ]
Hirano, T [1 ]
机构
[1] Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA
关键词
D O I
10.1126/science.282.5388.487
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
13S condensin is a multisubunit protein complex essential for mitotic chromosome condensation in Xenopus egg extracts. Purified 135 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 phospholylation, and peptide-mapping experiments indicated that Cdc2 is Likely to be the kinase that phosphorylates and activates 135 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 135 condensin by Cdc2 may trigger mitotic chromosome condensation in vitro.
引用
收藏
页码:487 / 490
页数:4
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