The identification of a functional interaction between PKC and topoisomerase II.
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.
Mouchel
Nathalie A P
NA
Compton Paddock Laboratories, Frilsham Home Farm Business Unit, Yattendon, Thatcham RG 18 0XT, UK.
Jenkins
John R
JR
D002118:Calcium / Q000378:metabolism; D047389:Casein Kinase I / Q000235:genetics / Q000378:metabolism*; D020090:Chromosome Segregation / Q000502:physiology; D004250:DNA Topoisomerases, Type II / Q000235:genetics / Q000378:metabolism*; D015530:Nuclear Matrix / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D029701:Saccharomyces cerevisiae Proteins; D047389:Casein Kinase I; D004250:DNA Topoisomerases, Type II; D002118:Calcium