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Vol. 15, Issue 4, 1711-1723, April 2004

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Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae

Chong J. Park ^*, Sukgil Song ^* , Thomas H. Giddings, Jr. , Hyeon-Su Ro ^* , Krisada Sakchaisri ^*, Jung-Eun Park ^*, Yeon-Sun Seong ^*, Mark Winey , and Kyung S. Lee ^* ||

^* Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892; Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347

Submitted July 2, 2003; Revised November 7, 2003; Accepted November 21, 2003
Monitoring Editor: Tim Stearns

The polo-box domain of the budding yeast polo kinase Cdc5p plays an essential role for targeting the catalytic activity of Cdc5p to spindle pole bodies (SPBs) and cytokinetic neck-filaments. Here, we report the isolation of Bbp1p as a polo-box interacting protein by a yeast two-hybrid screen. Bbp1p localizes to the periphery of the central plaque of the SPB and plays an important role in SPB duplication. Similarly, Cdc5p localized to the cytoplasmic periphery of the SPB. In vitro binding studies showed that Cdc5p interacted with the N-terminal domain of Bbp1p (Bbp1pC), but apparently not with Mps2p, a component shown to form a stable complex with Bbp1p. In addition, Bbp1p, but likely not Mps2p, was required for proper localization of Cdc5p to the SPB. The C-terminal coiled-coil domain of Bbp1p (Bbp1p^243–385), which is crucial for both the homodimerization and the SPB localization, could target the localization-defective Cdc5pC to the SPB and induce the release of Cdc14p from the nucleolus. Consistent with this observation, expression of CDC5C-BBP1^243–385 under CDC5 promoter control partially complemented the cdc5 defect. These data suggest that Bbp1pC interacts with the polo-box domain of Cdc5p, and this interaction is critical for the subcellular localization and mitotic functions of Cdc5p.

Present address: College of Pharmacy, Chungbuk National University, 48 Gaesin-dong, Cheongju, Chungbuk, South Korea

Present address: Laboratory of Integrative Biotechnology, Korea Research Institute of Bioscience and Biotechnology, 52 Oun-Dong, Yusong, Taejeon, South Korea.

^|| Corresponding author. E-mail address: kyunglee{at}pop.nci.nih.gov.

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