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J. Biol. Chem., Vol. 275, Issue 24, 18070-18078, June 16, 2000
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From the Department of Molecular Microbiology and Immunology,
University of Missouri, Columbia, Missouri 65212
Inhibitor-1 (I-1) is a specific inhibitor of
protein phosphatase-1 (PP1). We assayed the ability of I-1 to inhibit
Saccharomyces cerevisiae PP1, Glc7p, in
vivo. Glc7p like other PP1 catalytic subunits associates
with a variety of noncatalytic subunits, and Glc7p holoenzymes perform
distinct physiological roles. Our results show that I-1 inhibits Glc7p
holoenzymes that regulate transcription and mitosis, but holoenzymes
responsible for meiosis and glycogen metabolism were unaffected.
Additionally, we exploited a genetic screen for mutants that were
dependent on I-1 to grow. This scheme can identify processes that are
negatively regulated by Glc7p-catalyzed dephosphorylation. In this
paper I-1-dependent gfa1 mutations were
analyzed in detail. GFA1 encodes
glutamine-fructose-6-phosphate transaminase. One or more phosphorylated
proteins activate GFA1 transcription because the pheromone
response and Pkc1p/mitogen-activated protein kinase pathways positively
regulate GFA1 transcription. Our findings show that an
I-1-sensitive Glc7p holoenzyme reduces GFA1
transcription. Therefore, GFA1 is a member of a
growing list of genes that are negatively regulated by Glc7p dephosphorylation.
This paper is dedicated to Jeanne Cannon, 1939-1999.
Glc7p Protein Phosphatase Inhibits Expression of
Glutamine-Fructose-6-phosphate Transaminase from GFA1*
,
*
This work was supported in part by National Institutes of
Health Grant GM40326 (to J. F. C.) and funds from the Molecular Microbiology and Immunology Department, University of Missouri.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.
Supported in part by National Institutes of Health Training Grant AI07276.
§
To whom correspondence should be addressed: Dept. of Molecular
Microbiology and Immunology, M607 Medical Science Bldg., University of
Missouri, Columbia, MO 65212. Tel.: 573-882-2780; Fax: 573-882-4287; E-mail: CannonJ@missouri.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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