Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes

Cell. 2000 Aug 4;102(3):279-91. doi: 10.1016/s0092-8674(00)00034-9.


Phosphorylation of histone H3 at serine 10 occurs during mitosis and meiosis in a wide range of eukaryotes and has been shown to be required for proper chromosome transmission in Tetrahymena. Here we report that Ipl1/aurora kinase and its genetically interacting phosphatase, Glc7/PP1, are responsible for the balance of H3 phosphorylation during mitosis in Saccharomyces cerevisiae and Caenorhabditis elegans. In these models, both enzymes are required for H3 phosphorylation and chromosome segregation, although a causal link between the two processes has not been demonstrated. Deregulation of human aurora kinases has been implicated in oncogenesis as a consequence of chromosome missegregation. Our findings reveal an enzyme system that regulates chromosome dynamics and controls histone phosphorylation that is conserved among diverse eukaryotes.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aurora Kinases
  • Caenorhabditis elegans / cytology*
  • Caenorhabditis elegans / metabolism
  • Fungal Proteins / metabolism*
  • Genome
  • Helminth Proteins / metabolism
  • Histones / metabolism*
  • Mitosis*
  • Phenotype
  • Phosphoprotein Phosphatases / metabolism*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • RNA, Antisense
  • RNA, Small Interfering
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / metabolism
  • Serine / metabolism
  • Species Specificity


  • Fungal Proteins
  • Helminth Proteins
  • Histones
  • RNA, Antisense
  • RNA, Small Interfering
  • Serine
  • Aurora Kinases
  • Protein Serine-Threonine Kinases
  • Phosphoprotein Phosphatases