title: Spindle pole body components are reorganized during fission yeast meiosis.
abstract: During meiosis, the centrosome/spindle pole body (SPB) must be regulated in a manner distinct from that of mitosis to achieve a specialized cell division that will produce gametes. In this paper, we demonstrate that several SPB components are localized to SPBs in a meiosis-specific manner in the fission yeast Schizosaccharomyces pombe. SPB components, such as Cut12, Pcp1, and Spo15, which stay on the SPB during the mitotic cell cycle, disassociate from the SPB during meiotic prophase and then return to the SPB immediately before the onset of meiosis I. Interestingly, the polo kinase Plo1, which normally localizes to the SPB during mitosis, is excluded from them in meiotic prophase, when meiosis-specific, horse-tail nuclear movement occurs. We found that exclusion of Plo1 during this period was essential to properly remodel SPBs, because artificial targeting of Plo1 to SPBs resulted in an overduplication of SPBs. We also found that the centrin Cdc31 was required for meiotic SPB remodeling. Thus Plo1 and a centrin play central roles in the meiotic SPB remodeling, which is essential for generating the proper number of meiotic SPBs and, thereby provide unique characteristics to meiotic divisions.
authors.affiliation: Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan.
authors.forename: Midori
authors.initials: M
authors.lastname: Ohta
authors.forename: Masamitsu
authors.initials: M
authors.lastname: Sato
authors.forename: Masayuki
authors.initials: M
authors.lastname: Yamamoto
mesh_terms: D016203:CDC2 Protein Kinase / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism; D018385:Centrosome / Q000378:metabolism*; D020090:Chromosome Segregation; D049452:Green Fluorescent Proteins / Q000378:metabolism; D018386:Kinetochores / Q000378:metabolism; D020935:MAP Kinase Signaling System; D049469:Meiotic Prophase I; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012568:Schizosaccharomyces / Q000166:cytology / Q000378:metabolism* / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins / Q000378:metabolism*; D008941:Spindle Apparatus / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; C111708:Cut12 protein, S pombe; C507869:Hrs1 protein, S pombe; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D029702:Schizosaccharomyces pombe Proteins; C406741:Spo15 protein, S pombe; C489994:cdc31 protein, S pombe; C454082:pcp1 protein, S pombe; D049452:Green Fluorescent Proteins; C501407:Plo1 protein, S pombe; D017346:Protein Serine-Threonine Kinases; D016203:CDC2 Protein Kinase; C469447:cdc2 protein, S pombe; D020928:Mitogen-Activated Protein Kinases; C498189:Spk1 protein, S pombe