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Vol. 9, Issue 8, 2325-2335, August 1998
Institute of Cell and Molecular Biology, University of Edinburgh,
Edinburgh EH9 3JR, United Kingdom
The Schizosaccharomyces pombe win1-1 mutant has a
defect in the G2-M transition of the cell cycle. Although the defect is suppressed by wis1+ and
wis4+, which are components of a
stress-activated MAP kinase pathway that links stress response and cell
cycle control, the molecular identity of Win1 has not been known. We
show here that win1+ encodes a polypeptide
of 1436 residues with an apparent molecular size of 180 kDa and
demonstrate that Win1 is a MAP kinase kinase kinase that
phosphorylates and activates Wis1. Despite extensive similarities
between Win1 and Wis4, the two MAP kinase kinase kinases have distinct
functions. Wis4 is able to compensate for loss of Win1 only under
unstressed conditions to maintain basal Wis1 activity, but it fails to
suppress the osmosignaling defect conferred by win1
mutations. The win1-1 mutation is a spontaneous duplication of 16 nucleotides, which leads to a frameshift and production of a truncated protein lacking the kinase domain. We discuss
the cell cycle phenotype of the win1-1 cdc25-22 wee1-50 mutant and its suppression by wis genes.
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