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The budding yeast point centromere associates with two Cse4 molecules during mitosis.

The centromere is defined by the incorporation of the centromere-specific histone H3 variant centromere protein A (CENP-A). Like histone H3, CENP-A can form CENP-A-H4 heterotetramers in vitro. However, the in vivo conformation of CENP-A chromatin has been proposed by different studies as hemisomes, canonical, or heterotypic nucleosomes. A clear understanding of the in vivo architecture of CENP-A chromatin is important, because it influences the molecular mechanisms of the assembly and maintenance of the centromere and its function in kinetochore nucleation. A key determinant of this architecture is the number of CENP-A molecules bound to the centromere. Accurate measurement of this number can limit possible centromere architectures. The genetically defined point centromere in the budding yeast Saccharomyces cerevisiae provides a unique opportunity to define this number accurately, as this 120-bp-long centromere can at the most form one nucleosome or hemisome. Using novel live-cell fluorescence microscopy assays, we demonstrate that the budding yeast centromere recruits two Cse4 (ScCENP-A) molecules. These molecules are deposited during S phase and they remain stably bound through late anaphase. Our studies suggest that the budding yeast centromere incorporates a Cse4-H4 tetramer.

Pubmed ID: 23623551

Authors

  • Aravamudhan P
  • Felzer-Kim I
  • Joglekar AP

Journal

Current biology : CB

Publication Data

May 6, 2013

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM105948

Mesh Terms

  • Anaphase
  • Autoantigens
  • Centromere
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • Histones
  • Kinetochores
  • Microscopy, Fluorescence
  • Mitosis
  • Nucleosomes
  • Protein Conformation
  • S Phase
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins