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J Biol Chem, Vol. 273, Issue 50, 33311-33319, December 11, 1998
From the In the yeast Saccharomyces
cerevisiae, trehalose-6-phosphate synthase (TPS) and
trehalose-6-phosphate phosphatase (TPP), which convert glucose
6-phosphate plus UDP-glucose to trehalose, are part of the trehalose
synthase complex. In addition to the TPS1 (previously also
called GGS1, CIF1, BYP1,
FDP1, GLC6, and TSS1) and
TPS2 (also described as HOG2 and
PFK3) gene products, this complex also contains a
regulatory subunit encoded by TSL1. We have constructed a
set of isogenic strains carrying all possible combinations of deletions
of these three genes and of TPS3, a homologue of
TSL1 identified by systematic sequencing. Deletion of
TPS1 totally abolished TPS activity and measurable
trehalose, whereas deletion of any of the other genes in most cases
reduced both. Similarly, deletion of TPS2 completely
abolished TPP activity, and deletion of any of the other genes resulted
in a reduction of this activity. Therefore, it appears that all
subunits are required for optimal enzymatic activity. Since we observed
measurable trehalose in strains lacking all but the TPS1
gene, some phosphatase activity in addition to Tps2 can hydrolyze
trehalose 6-phosphate. Deletion of TPS3, in particular in a
tsl1
Composition and Functional Analysis of the Saccharomyces
cerevisiae Trehalose Synthase Complex
,,,,
Laboratorium voor Moleculaire Celbiologie,
Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001
Leuven-Heverlee, Flanders, Belgium and the ¶ Botanisches Institut
der Universität, Hebelstrasse 1, CH-4056 Basel, Switzerland
background, reduced both TPS and TPP activities and
trehalose content. Deletion of TPS2, TSL1, or
TPS3 and, in particular, of TSL1 plus
TPS3 destabilized the trehalose synthase complex. We
conclude that Tps3 is a fourth subunit of the complex with functions
partially redundant to those of Tsl1. Among the four genes studied,
TPS1 is necessary and sufficient for growth on glucose and
fructose. Even when overproduced, none of the other subunits could take
over this function of Tps1 despite the homology shared by all four
proteins. A portion of Tps1 appears to occur in a form not bound by the
complex. Whereas TPS activity in the complex is inhibited by
Pi, Pi stimulates the monomeric form of Tps1.
We discuss the possible role of differentially regulated Tps1 in a
complex-bound or monomeric form in light of the requirement of Tps1 for
trehalose production and for growth on glucose and fructose.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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