Interaction of chromatin-associated Plk1 and Mcm7

被引：47

作者：

Tsvetkov, L ^{[1
]}

Stern, DF ^{[1
]}

机构：

[1] Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06511 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2005年 / 280卷 / 12期

关键词：

D O I：

10.1074/jbc.M413514200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Plk1 is a multifunctional protein kinase involved in regulation of mitotic entry, chromosome segregation, centrosome maturation, and mitotic exit. Plk1 is a target of DNA damage checkpoints and aids resumption of the cell cycle during recovery from G(2) arrest. The polo-box domain (PBD) of Plk1 interacts with phosphoproteins and localizes Plk1 to some mitotic structures. In a search for proteins that interact with the PBD of Plk1, we identified two of the minichromosome maintenance (MCM) proteins, Mcm2 and Mcm7. Co-immunoprecipitation and immunoblot analysis showed an interaction between full-length Plk1 and all other members of the MCM2-7 protein complex. Endogenous Plk1 co-immunoprecipitates with basal forms of Mcm7 as well as with slower migrating forms of Mcm7, induced in response to DNA damage. The strongest interaction between endogenous Plk1 and Mcm7 was detected in a soluble chromatin fraction. These findings suggest a new function for Plk1 in coordination of DNA replication and mitotic events.

引用

页码：11943 / 11947

页数：5

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