Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans.

Abstract:

: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.

journal_name

Cell

journal_title

Cell

authors

De Souza CP,Osmani AH,Wu LP,Spotts JL,Osmani SA

doi

10.1016/s0092-8674(00)00035-0

subject

Has Abstract

pub_date

2000-08-04 00:00:00

pages

293-302

issue

3

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)00035-0

journal_volume

102

pub_type

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