| Summary: | The polo-like kinases are a family of highly conserved serine/threonine protein kinases with multiple mitotic functions. Polo-like kinases are recognisable by the presence of two conserved domains: a catalytic, kinase domain at the amino terminus of the protein and at the carboxy terminus, a non-catalytic domain. In the fission yeast, <i>Schizosaccharomyces pombe</i>, there is one member of this family, Plol. The aim of this study was to define the function of the non-catalytic domain of the protein and to identify unknown mitotic roles for Plol. Site directed mutagenesis of Plol illustrated the roles of the two conserved domains in different aspects of the Plol function. Localisation, regulation of kinase activity and <i>in vivo</i> function of mutant proteins were analysed. Two hybrid analysis was carried out to identify interacting proteins. This was successful in revealing previously uncharacterised functions for Plol such as an interaction with the anaphase promoting complex subunit, Cut23. Reverse two hybrid screening combined with random mutagenesis was carried out to determine the <i>in vivo</i> consequences of eliminating specific interactions.
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