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J. Biol. Chem., Vol. 276, Issue 18, 14549-14552, May 4, 2001
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From the The p21-activated kinase, Shk1, is
required for cell viability, establishment and maintenance of cell
polarity, and proper mating response in the fission yeast,
Schizosaccharomyces pombe. Previous genetic studies
suggested that a presumptive protein methyltransferase, Skb1, functions
as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not
required for viability or mating of S. pombe cells and
contributes only modestly to the regulation of cell morphology under
normal growth conditions. Here we demonstrate that Skb1 plays a more
significant role in regulating cell growth and polarity under
conditions of hyperosmotic stress. We provide evidence that the
inability of skb1
ACCELERATED PUBLICATION
The Highly Conserved Protein Methyltransferase, Skb1, Is a
Mediator of Hyperosmotic Stress Response in the Fission Yeast
Schizosaccharomyces pombe*
§,§,§,,,,,,
Department of Molecular Genetics and the
Graduate Program in Genes and Development, University of Texas, M. D. Anderson Cancer Center, Houston, Texas 77030 and the ¶ Department
of Biochemistry and Molecular Biology, University of Miami, School of
Medicine, Miami, Florida 33136-1015
cells to properly maintain cell
polarity in hyperosmotic conditions results from inefficient
subcellular targeting of F-actin. We show that Skb1 localizes to cell
ends, sites of septation, and nuclei of S. pombe cells.
Hyperosmotic shock results in substantial delocalization of Skb1 from
cell ends and nuclei, as well as stimulation of Skb1 protein
methyltransferase activity. Taken together, our results demonstrate a
new role for Skb1 as a mediator of hyperosmotic stress response in
fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by
hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as
mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.
*
This research was supported by National Institutes of Health
Grant R01GM53239 (to S. M.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
713-745-2032; Fax: 713-794-4394; E-mail: smarcus@mdacc.tmc.edu.
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