Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.
Hsu JY,
Sun ZW,
Li X,
Reuben M,
Tatchell K,
Bishop DK,
Grushcow JM,
Brame CJ,
Caldwell JA,
Hunt DF,
Lin R,
Smith MM,
Allis CD.
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville 22908, USA.
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.
PMID: 10975519 [PubMed - indexed for MEDLINE]