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MBC in Press, published online ahead of print February 6, 2004
Mol. Biol. Cell 10.1091/mbc.E03-07-0461

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Submitted on July 2, 2003
Revised on November 7, 2003
Accepted on November 21, 2003

Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in S. cerevisiae

Chong J. Park1, Sukgil Song2, Thomas H. Giddings Jr.3, Hyeon-Su Ro4, Krisada Sakchaisri1, Jung-Eun Park1, Yeon-Sun Seong1, Mark Winey3, and Kyung S. Lee1*

1 Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, 9000 Rockville Pike, Bldg. 37, Rm. 2D11, Bethesda, MD 20892
2 Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, 9000 Rockville Pike, Bldg. 37, Rm. 2D11, Bethesda, MD 20892, College of Pharmacy, Chungbuk National University, 48 Gaesin-dong, Cheongju, Chungbuk, South Korea
3 Department of Molecular, Cellular, and Developmental Biology, CB 347, University of Colorado, Boulder, CO 80309-0347
4 Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, 9000 Rockville Pike, Bldg. 37, Rm. 2D11, Bethesda, MD 20892, 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.

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 (Bbp1p{Delta}C), 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 (Bbp1p243-385), which is crucial for both the homo-dimerization and the SPB localization, could target the localization-defective Cdc5p{Delta}C to the SPB and induce the release of Cdc14p from the nucleolus. Consistent with this observation, expression of CDC5{Delta}C-BBP1243-385 under CDC5 promoter control partially complemented the cdc5{Delta} defect. These data suggest that Bbp1p{Delta}C interacts with the polo-box domain of Cdc5p, and this interaction is critical for the subcellular localization and mitotic functions of Cdc5p.




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