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J. Biol. Chem., Vol. 276, Issue 10, 7027-7032, March 9, 2001
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From the Department of Molecular Microbiology and Biotechnology,
Faculty of Life Sciences. Tel Aviv University, Tel
Aviv 69978, Israel
Targets of rapamycin (TORs) are conserved
phosphatidylinositol kinase-related kinases that are involved in the
coordination between nutritional or mitogenic signals and cell growth.
Here we report the initial characterization of two
Schizosaccharomyces pombe TOR homologs,
tor1+ and tor2+.
tor2+ is an essential gene, whereas
tor1+ is required only under starvation and
other stress conditions. Specifically,
The Fission Yeast TOR Homolog,
tor1+, Is Required for the Response to
Starvation and Other Stresses via a Conserved Serine*
and
tor1 cells fail
to enter stationary phase or undergo sexual development and are
sensitive to cold, osmotic stress, and oxidative stress. In complex
with the prolyl isomerase FKBP12, the drug rapamycin binds a conserved
domain in TORs, FRB, thus inhibiting some of the functions of TORs.
Mutations at a conserved serine within the FRB domain of
Saccharomyces cerevisiae TOR proteins led to rapamycin
resistance but did not otherwise affect the functions of the proteins.
The S. pombe tor1+ exhibits different features;
substitution of the conserved serine residue, Ser1834, with
arginine compromises its functions and has no effect on the inhibition
that rapamycin exerts on sexual development in S. pombe.
*
This work was supported by a Israel Cancer Research Found
fellowship (to R. W.) and by a Ela Kodesz Institute for Research on Cancer Development and Prevention grant (to M. C.).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.: 972-3-0407532;
Fax: 972-3-6409407; E-mail: ronitt@post.tau.ac.il.
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