title: Dyskerin, tRNA genes, and condensin tether pericentric chromatin to the spindle axis in mitosis.
abstract: Condensin is enriched in the pericentromere of budding yeast chromosomes where it is constrained to the spindle axis in metaphase. Pericentric condensin contributes to chromatin compaction, resistance to microtubule-based spindle forces, and spindle length and variance regulation. Condensin is clustered along the spindle axis in a heterogeneous fashion. We demonstrate that pericentric enrichment of condensin is mediated by interactions with transfer ribonucleic acid (tRNA) genes and their regulatory factors. This recruitment is important for generating axial tension on the pericentromere and coordinating movement between pericentromeres from different chromosomes. The interaction between condensin and tRNA genes in the pericentromere reveals a feature of yeast centromeres that has profound implications for the function and evolution of mitotic segregation mechanisms.
authors.affiliation: Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
authors.forename: Chloe E
authors.initials: CE
authors.lastname: Snider
authors.affiliation: Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Stephens
authors.affiliation: Molecular, Cell and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064.
authors.forename: Jacob G
authors.initials: JG
authors.lastname: Kirkland
authors.affiliation: Molecular, Cell and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064.
authors.forename: Omar
authors.initials: O
authors.lastname: Hamdani
authors.affiliation: Molecular, Cell and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064.
authors.forename: Rohinton T
authors.initials: RT
authors.lastname: Kamakaka
authors.affiliation: Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 Kerry_Bloom@unc.edu.
authors.forename: Kerry
authors.initials: K
authors.lastname: Bloom
mesh_terms: D000251:Adenosine Triphosphatases / Q000032:analysis / Q000378:metabolism*; D018385:Centrosome / Q000378:metabolism / Q000648:ultrastructure; D002843:Chromatin / Q000378:metabolism* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000032:analysis / Q000378:metabolism*; D006836:Hydro-Lyases / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D018386:Kinetochores / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D008938:Mitosis / Q000502:physiology*; D046912:Multiprotein Complexes / Q000032:analysis / Q000378:metabolism*; D012343:RNA, Transfer / Q000235:genetics*; D017411:Ribonucleoproteins, Small Nuclear / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000166:cytology*; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D008941:Spindle Apparatus / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D002843:Chromatin; D004268:DNA-Binding Proteins; D008869:Microtubule-Associated Proteins; D046912:Multiprotein Complexes; D017411:Ribonucleoproteins, Small Nuclear; D029701:Saccharomyces cerevisiae Proteins; C108312:condensin complexes; D012343:RNA, Transfer; D000251:Adenosine Triphosphatases; D006836:Hydro-Lyases; C082278:CBF5 protein, S cerevisiae