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FEBS Lett. 2006 Jan 9;580(1):51-7. Epub 2005 Dec 9.

The identification of a functional interaction between PKC and topoisomerase II.

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  • 1Compton Paddock Laboratories, Frilsham Home Farm Business Unit, Yattendon, Thatcham RG 18 0XT, UK.


Topoisomerase II plays an essential role in the segregation of chromosomes during cell division. It is also a major component of the nuclear matrix. Proteins that interact with and regulate this essential enzyme are of great interest. To investigate the role of proteins interacting with the N-terminal domain of the Saccharomyces cerevisiae topoisomerase II, we used a yeast two-hybrid protein interaction screen. We identified an interaction between the catalytic domain of the yeast protein kinase 1 enzyme (Pkc1) and the N-terminal domain of the S. cerevisiae topoisomerase II. The S. cerevisiae Pkc1 is the homologue of the mammalian calcium dependent PKC.

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