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The identification of a functional interaction between PKC and topoisomerase II
Author(s) -
Mouchel Nathalie A.P.,
Jenkins John R.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.075
Subject(s) - saccharomyces cerevisiae , topoisomerase , yeast , enzyme , domain (mathematical analysis) , biochemistry , protein kinase c , chemistry , microbiology and biotechnology , biology , mathematical analysis , mathematics
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.