An SMC-domain protein in fission yeast links telomeres to the meiotic centrosome

Mark R. Flory, Andrew R. Carson, Eric G. Muller, Ruedi Aebersold

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Abnormal centrosomal structures similar to those occurring in human cancers are induced in fission yeast by overexpression of the pericentrin homolog Pcp1p. Analysis of abnormal Pcp1p-containing structures with quantitative mass spectrometry and isotope-coded affinity tags identified a coiled-coil, structural maintenance of chromosomes (SMC) domain protein. This protein, termed Ccq1p (coiled-coil protein quantitatively enriched), localizes with Taz1p to telomeres in normal vegetative cells. Fluorescence resonance energy transfer (FRET) measurements indicate that Ccq1p also interacts with centrosomal Pcp1p in mating pheromone-stimulated cells containing centrosomally clustered telomeres. We provide evidence that the Ccq1p-Pcp1p interaction, while essential for meiosis, is deleterious when forced to occur during vegetative growth. Cells lacking one ccq1 allele exhibit a loss-of-function phenotype including abnormally long cell length, chromosome segregation failure, telomeric shortening, and defective telomeric clustering during meiotic prophase. Our data indicate a mechanism underlying meiotic chromosomal bouquet formation and suggest a recruitment model for supernumerary centrosome toxicity.

Original languageEnglish (US)
Pages (from-to)619-630
Number of pages12
JournalMolecular Cell
Volume16
Issue number4
DOIs
StatePublished - Nov 19 2004

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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