Affiliation:
1. Department of Bacteriology and Public Health, Washington State University, Pullman, Washington 99163
Abstract
The properties of a specific system for the transport of
S
-adenosylmethionine in yeast are described. The process was
p
H-, temperature-, and energy-dependent, and showed saturation kinetics. The
K
m
for the system was 3.3 × 10
−6
m
. Of the
S
-adenosylmethionine moieties tested, only
S
-adenosylhomocysteine competitively inhibited the uptake of the adenosylsulfonium compound. Adenine, adenosine, methionine, homocysteine, and the sulfonium compound
S
-methylmethionine were without effect. The analogue
S
-adenosylethionine showed competitive inhibition. Under conditions of inhibition of protein synthesis by cycloheximide or methionine starvation, permease activity was stable. The mutant
sam-p3
apparently was able to transport
S
-adenosylmethionine only by diffusion. Uptake by diploids containing this mutation was directly proportional to the gene dose.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
38 articles.
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