Affiliation:
1. The Department of Physiological Chemistry, University of Wisconsin Medical School, Madison, Wisconsin 53706
Abstract
ABSTRACT
Mutants resistant to selenomethionine were isolated, and their properties studied. Mapping studies indicate that the mutation sites are located near the eth-1r locus in linkage group I, about ten map units away from the mating type locus. The sites of new mutation are either allelic to or very close to eth-1r. They are resistant not only to selenomethionine but also to ethionine, while the ethionine-resistant mutant, eth-1r, is sensitive to selenomethionine. The selenomethionine-resistant mutants are also temperature-sensitive mutants. However, they can grow at higher temperatures in medium containing 1 M glycerol.—It is very unlikely that the resistance is due to a change in the permeability of the membrane. Aryl sulfatase of se-metr mutants is not repressed by a high concentration of methionine (5 mM), although inorganic sulfate (2 mM) still can cause total repression. The γ-cystathionase levels of the mutants are normal, but the S-adenosylmethionine synthetase levels are only one-tenth of that observed in the wild-type strain. The heat-stability of this enzyme in the mutant is also different from that of the wild-type enzyme suggesting that the mutation might affect the structural gene of S-adenosylmethionine synthetase.
Publisher
Oxford University Press (OUP)
Cited by
4 articles.
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