Nature 363, 637 - 640 (17 June 1993); doi:10.1038/363637a0

A conserved mitotic kinase active at late anaphase—telophase in syncytial Drosophila embryos

Brian Fenton^* & David M. Glover

Cancer Research Campaign Cell Cycle Genetics Group, Department of Anatomy and Physiology, Medical Sciences Institute, University of Dundee, Dundee DD14HN, UK
^*Present address: Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, UK.

MUTATIONS in the Drosophila gene polo cause abnormal mitotic and meiotic divisions^1,2. This gene encodes a 577-amino-acid protein that has an N-terminal putative kinase domain and a 300-residue C-terminal domain2. In budding yeast, a homolo-gous kinase is encoded by CDC5 (ref. 3), a gene required for nuclear division late in the mitotic cycle⁴ and during meiosis⁵. Murine homologues have also been described^6,7. Here we show that the polo gene product immunoprecipitated from extracts of single Drosophila embryos can phosphorylate casein in vitro, and that the kinase activity peaks cyclically at late anaphase/telophase. This contrasts with the cyclical activity of cyclin B-associated p34^cdc2 kinase, which is maximal upon entry into mitosis during the rapid cycles of mitosis in the syncytium.

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