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Mol. Cell. Biol., 12 1996, 6752-6764, Vol 16, No. 12
T Toda, S Dhut, G Superti-Furga, Y Gotoh, E Nishida, R Sugiura and T Kuno
We have isolated a gene, pmk1+, a third mitogen-activated protein kinase
(MAPK) gene homolog from the fission yeast Schizosaccharomyces pombe. The
predicted amino acid sequence shows the most homology (63 to 65% identity)
to those of budding yeast Saccharomyces Mpk1 and Candida Mkc1. The Pmk1
protein contains phosphorylated tyrosines, and the level of tyrosine
phosphorylation was increased in the dsp1 mutant which lacks an attenuating
phosphatase for Pmk1. The level of tyrosine phosphorylation appears
constant during hypotonic or heat shock treatment. The cells with pmk1
deleted (delta pmk1) are viable but show various defective phenotypes,
including cell wall weakness, abnormal cell shape, a cytokinesis defect,
and altered sensitivities to cations, such as hypersensitivity to potassium
and resistance to sodium. Consistent with a high degree of conservation of
amino acid sequence, multicopy plasmids containing the MPK1 gene rescued
the defective phenotypes of the delta pmk1 mutant. The frog MAPK gene also
suppressed the pmk1 disruptant. The results of genetic analysis indicated
that Pmk1 lies on a novel MAPK pathway which does not overlap functionally
with the other two MAPK pathways, the Spk1-dependent mating signal pathway
and Sty1/Spc1/Phh1-dependent stress-sensing pathway. In Saccharomyces
cerevisiae, Mpk1 is involved in cell wall integrity and functions
downstream of the protein kinase C homolog. In contrast, in S. pombe, Pmk1
may not act in a linear manner with respect to fission yeast protein kinase
C homologs. Interestingly, however, these two pathways are not independent;
instead, they regulate cell integrity in a coordinate manner.
Copyright © 1996, American Society for Microbiology
The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway
Cell Regulation Laboratory, Imperial Cancer Research Fund, London, United Kingdom. toda@europa.lif.icnet.uk
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