title: pkl1(+)and klp2(+): Two kinesins of the Kar3 subfamily in fission yeast perform different functions in both mitosis and meiosis.
abstract: We have identified Klp2p, a new kinesin-like protein (KLP) of the KAR3 subfamily in fission yeast. The motor domain of this protein is 61% identical and 71% similar to Pkl1p, another fission yeast KAR3 protein, yet the two enzymes are different in behavior and function. Pkl1p is nuclear throughout the cell cycle, whereas Klp2p is cytoplasmic during interphase. During mitosis Klp2p enters the nucleus where it forms about six chromatin-associated dots. In metaphase-arrested cells these migrate back and forth across the nucleus. During early anaphase they segregate with the chromosomes into two sets of about three, fade, and are replaced by other dots that form on the spindle interzone. Neither klp2(+) nor pkl1(+) is essential, and the double deletion is also wild type for both vegetative and sexual reproduction. Each deletion rescues different alleles of cut7(ts), a KLP that contributes to spindle formation and elongation. When either or both deletions are combined with a dynein deletion, vegetative growth is normal, but sexual reproduction fails: klp2 Delta,dhc1-d1 in karyogamy, pkl1 Delta,dhc1-d1 in multiple phases of meiosis, and the triple deletion in both. Deletion of Klp2p elongates a metaphase-arrested spindle, but pkl1 Delta shortens it. The anaphase spindle of klp2 Delta becomes longer than the cell, leading it to curl around the cell's ends. Apparently, Klp2p promotes spindle disassembly and contributes to the behavior of mitotic chromosomes.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA.
authors.forename: C L
authors.initials: CL
authors.lastname: Troxell
authors.forename: M A
authors.initials: MA
authors.lastname: Sweezy
authors.forename: R R
authors.initials: RR
authors.lastname: West
authors.forename: K D
authors.initials: KD
authors.lastname: Reed
authors.forename: B D
authors.initials: BD
authors.lastname: Carson
authors.forename: A L
authors.initials: AL
authors.lastname: Pidoux
authors.forename: W Z
authors.initials: WZ
authors.lastname: Cande
authors.forename: J R
authors.initials: JR
authors.lastname: McIntosh
mesh_terms: D000483:Alleles; D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000235:genetics; D004398:Dyneins / Q000235:genetics; D005656:Fungal Proteins / Q000145:classification / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D005800:Genes, Fungal; D016547:Kinesins / Q000145:classification / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008540:Meiosis / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics; D008869:Microtubule-Associated Proteins / Q000235:genetics*; D008938:Mitosis / Q000502:physiology*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D010750:Phosphoproteins / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins; D017386:Sequence Homology, Amino Acid; D008941:Spindle Apparatus; D013696:Temperature; D013827:Thiabendazole / Q000494:pharmacology
chemical_list: D018797:Cell Cycle Proteins; C115450:Cut11 protein, S pombe; C111708:Cut12 protein, S pombe; C104159:Cut7 protein, S pombe; D005656:Fungal Proteins; C063504:KAR3 protein, S cerevisiae; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; C104160:PKL1 protein, S pombe; D010750:Phosphoproteins; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; D004398:Dyneins; D016547:Kinesins; D013827:Thiabendazole