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J Biol Chem, Vol. 273, Issue 51, 34454-34462, December 18, 1998
From the Biology Department, Queens College and the Graduate School
of the City University of New York, Flushing, New York 11367
In Saccharomyces, the addition of
glucose induces a rapid degradation of maltose permease that is
dependent on endocytosis and vacuolar proteolysis (Medintz, I., Jiang,
H., Han, E. K., Cui, W., and Michels, C. A. (1996) J. Bacteriol. 178, 2245-2254). Here we report on the role of
ubiquitin conjugation in this process. Deletion of DOA4,
which causes decreased levels of available ubiquitin, severely
decreases the rate of glucose-induced proteolysis, and this is
suppressed by the overproduction of ubiquitin. Overexpression of
ubiquitin in an endocytosis-deficient end3-ts strain
results in the glucose-stimulated accumulation of a larger molecular
weight species of maltose permease, which we demonstrate is a
ubiquitin-modified form of the protein by utilizing two ubiquitin
alleles with different molecular weights. The size of this
ubiquitinated species of maltose permease is consistent with
monoubiquitination. A promoter mutation that reduces expression of
RSP5/NPI1, a postulated ubiquitin-protein ligase, dramatically reduces the rate of glucose-induced proteolysis of
maltose permease. The role of various ubiquitin-conjugating enzymes was
investigated using strains carrying mutant alleles ubc1
ubc4, ubc4 ubc5,
cdc34-ts2/ubc3, and ubc9-ts. Loss
of these functions was not shown to effect glucose-induced proteolysis of maltose permease, but loss of Ubc1, -4, and -5 was found to inhibit
maltose permease expression at the post-transcriptional level.
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