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J. Cell Biol.,
Volume 141, Number 7, June 29, 1998 1575-1587

* Henry Hood Research Program, Weis Center for Research, Pennsylvania State University College of Medicine, Danville,
Pennsylvania 17822-2617; and NIMA promotes entry into mitosis in late G2
by some mechanism that is after activation of the
Aspergillus nidulans G2 cyclin-dependent kinase,
NIMXCDC2/NIMECyclin B. Here we present two independent lines of evidence which indicate that this mechanism involves control of NIMXCDC2/NIMECyclin B localization. First, we found that NIMECyclin B localized to
the nucleus and the nucleus-associated organelle, the
spindle pole body, in a NIMA-dependent manner.
Analysis of cells from asynchronous cultures, synchronous cultures, and cultures arrested in S or G2 showed
that NIMECyclin B was predominantly nuclear during interphase, with maximal nuclear accumulation in late
G2. NIMXCDC2 colocalized with NIMECyclin B in G2
cells. Although inactivation of NIMA using either the
nimA1 or nimA5 temperature-sensitive mutations
blocked cells in G2, NIMXCDC2/NIMECyclin B localization was predominantly cytoplasmic rather than nuclear. Second, we found that nimA interacts genetically
with sonA, which is a homologue of the yeast nucleocytoplasmic transporter GLE2/RAE1. Mutations in sonA
were identified as allele-specific suppressors of nimA1.
The sonA1 suppressor alleviated the nuclear division and NIMECyclin B localization defects of nimA1 cells
without markedly increasing NIMXCDC2 or NIMA kinase activity. These results indicate that NIMA promotes the nuclear localization of the NIMXCDC2/
NIMECyclin B complex, by a process involving SONA.
This mechanism may be involved in coordinating the
functions of NIMXCDC2 and NIMA in the regulation of
mitosis.
Molecular and Cellular Biology Section, School of Biological Sciences, University of Kentucky,
Lexington, Kentucky 40506-0225
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