Mitotic phosphorylation of histone H3 is governed by IpI1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes

Jer Yuan Hsu, Zu Wen Sun, Xiumin Li, Melanie Reuben, Kelly Tatchell, Douglas K. Bishop, Jeremy M. Grushcow, Cynthia J. Brame, Jennifer A. Caldwell, Donald F. Hunt, Rueyling Lin, M. Mitchell Smith, C. David Allis

Research output: Contribution to journalArticlepeer-review

731 Scopus citations

Abstract

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 IpI1/aurora kinase and its genetically interacting phosphatase, GIc7/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.

Original languageEnglish (US)
Pages (from-to)279-291
Number of pages13
JournalCell
Volume102
Issue number3
DOIs
StatePublished - Aug 4 2000

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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