Affiliation:
1. Department of Bacteriology and Public Health, Washington State University, Pullman, Washington 99163
Abstract
Two methionine biosynthetic enzymes and the methionine adenosyltransferase are repressed in
Saccharomyces cerevisiae
when grown under conditions where the intracellular levels of
S
-adenosylmethionine are high. The nature of the co-repressor molecule of this repression was investigated by following the intracellular levels of methionine,
S
-adenosylmethionine, and
S
-adenosylhomocysteine, as well as enzyme activities, after growth under various conditions. Under all of the conditions found to repress these enzymes, there is an accompanying induction of the
S
-adenosylmethionine-homocysteine methyltransferase which suggests that this enzyme may play a key role in the regulation of
S
-adenosylmethionine and methionine balance and synthesis.
S
-methylmethionine also induces the methyltransferase, but unlike
S
-adenosylmethionine, it does not repress the methionine adenosyltransferase or other methionine biosynthetic enzymes tested.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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