title: Ipl1/Aurora B kinase coordinates synaptonemal complex disassembly with cell cycle progression and crossover formation in budding yeast meiosis.
abstract: Several protein kinases collaborate to orchestrate and integrate cellular and chromosomal events at the G2/M transition in both mitotic and meiotic cells. During the G2/M transition in meiosis, this includes the completion of crossover recombination, spindle formation, and synaptonemal complex (SC) breakdown. We identified Ipl1/Aurora B kinase as the main regulator of SC disassembly. Mutants lacking Ipl1 or its kinase activity assemble SCs with normal timing, but fail to dissociate the central element component Zip1, as well as its binding partner, Smt3/SUMO, from chromosomes in a timely fashion. Moreover, lack of Ipl1 activity causes delayed SC disassembly in a cdc5 as well as a CDC5-inducible ndt80 mutant. Crossover levels in the ipl1 mutant are similar to those observed in wild type, indicating that full SC disassembly is not a prerequisite for joint molecule resolution and subsequent crossover formation. Moreover, expression of meiosis I and meiosis II-specific B-type cyclins occur normally in ipl1 mutants, despite delayed formation of anaphase I spindles. These observations suggest that Ipl1 coordinates changes to meiotic chromosome structure with resolution of crossovers and cell cycle progression at the end of meiotic prophase.
authors.affiliation: Medical Research Council Genome Damage and Stability Centre, University of Sussex, Falmer BN1 9RQ, United Kingdom.
authors.forename: Philip
authors.initials: P
authors.lastname: Jordan
authors.forename: Alice
authors.initials: A
authors.lastname: Copsey
authors.forename: Louise
authors.initials: L
authors.lastname: Newnham
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Kolar
authors.forename: Michael
authors.initials: M
authors.lastname: Lichten
authors.forename: Eva
authors.initials: E
authors.lastname: Hoffmann
mesh_terms: D064127:Aurora Kinases; D002453:Cell Cycle / Q000187:drug effects; D018797:Cell Cycle Proteins / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism*; D007976:Leupeptins / Q000494:pharmacology; D008540:Meiosis / Q000235:genetics / Q000502:physiology*; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D011995:Recombination, Genetic / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000201:enzymology / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013573:Synaptonemal Complex / Q000378:metabolism*
chemical_list: D018797:Cell Cycle Proteins; D015853:Cysteine Proteinase Inhibitors; D047908:Intracellular Signaling Peptides and Proteins; D007976:Leupeptins; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; C090118:Zip1 protein, S cerevisiae; D011494:Protein Kinases; D064127:Aurora Kinases; C576961:IPL1 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases; C081927:CDC5 protein, S cerevisiae; C072553:benzyloxycarbonylleucyl-leucyl-leucine aldehyde