Literature DB >> 16364307

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

Nathalie A P Mouchel1, John R Jenkins.   

Abstract

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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Year:  2005        PMID: 16364307     DOI: 10.1016/j.febslet.2005.11.075

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  The Aurora B specificity switch is required to protect from non-disjunction at the metaphase/anaphase transition.

Authors:  Joanna R Kelly; Silvia Martini; Nicola Brownlow; Dhira Joshi; Stefania Federico; Shirin Jamshidi; Svend Kjaer; Nicola Lockwood; Khondaker Miraz Rahman; Franca Fraternali; Peter J Parker; Tanya N Soliman
Journal:  Nat Commun       Date:  2020-03-13       Impact factor: 14.919

  1 in total

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