Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans

Cell. 2000 Aug 4;102(3):293-302. doi: 10.1016/s0092-8674(00)00035-0.


Phosphorylation of histone H3 serine 10 correlates with chromosome condensation and is required for normal chromosome segregation in Tetrahymena. This phosphorylation is dependent upon activation of the NIMA kinase in Aspergillus nidulans. NIMA expression also induces Ser-10 phosphorylation inappropriately in S phase-arrested cells and in the absence of NIMX(cdc2) activity. At mitosis, NIMA becomes enriched on chromatin and subsequently localizes to the mitotic spindle and spindle pole bodies. The chromatin-like localization of NIMA early in mitosis is tightly correlated with histone H3 phosphorylation. Finally, NIMA can phosphorylate histone H3 Ser-10 in vitro, suggesting that NIMA is a mitotic histone H3 kinase, perhaps helping to explain how NIMA promotes chromatin condensation in A. nidulans and when expressed in other eukaryotes.

Publication types

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

MeSH terms

  • Aspergillus nidulans / cytology*
  • Aspergillus nidulans / metabolism
  • CDC2 Protein Kinase / metabolism
  • Cell Compartmentation
  • Cell Cycle Proteins*
  • Chromatin / enzymology
  • Chromosomes, Fungal / genetics
  • Histones / metabolism*
  • Microtubules / enzymology
  • Mitosis*
  • NIMA-Related Kinase 1
  • NIMA-Related Kinases
  • Phosphorylation
  • Protein-Serine-Threonine Kinases / isolation & purification
  • Protein-Serine-Threonine Kinases / metabolism*
  • Serine / metabolism
  • Spindle Apparatus / enzymology


  • Cell Cycle Proteins
  • Chromatin
  • Histones
  • Serine
  • NIMA-Related Kinase 1
  • NIMA-Related Kinases
  • NIMA-related kinase 6
  • Protein-Serine-Threonine Kinases
  • CDC2 Protein Kinase