Mitotic Histone H3 Phosphorylation by the NIMA Kinase in Aspergillus nidulans

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 inapprop...

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Bibliographic Details
Published in:Cell 2000-08, Vol.102 (3), p.293-302
Main Authors: De Souza, Colin P.C, Osmani, Aysha H, Wu, Li-Ping, Spotts, Jeffrey L, Osmani, Stephen A
Format: Article
Language:English
Subjects:
Aspergillus nidulans
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 kinase
NIMA-Related Kinase 1
NIMA-Related Kinases
Phosphorylation
Protein-Serine-Threonine Kinases - isolation & purification
Protein-Serine-Threonine Kinases - metabolism
Serine - metabolism
Spindle Apparatus - enzymology
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Summary: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.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)00035-0