Affiliation:
1. Department of Biochemistry, Purdue University, Lafayette, Indiana 47907
Abstract
Eighteen mutants (designated MT
s
), isolated in
Escherichia coli
K-12, showed increased sensitivity to inhibition of growth by 5-methyltryptophan. All mutants were also much more sensitive to 4-methyltryptophan and 7-azatryptophan but exhibited near normal sensitivity to 5-fluorotryptophan and 6-fluorotryptophan. All of the mutations were linked to the
trp
operon. Their locations within the
trp
operon were established by deletion mapping. There was good agreement between the map position of an MT
s
mutation and a lowered activity of one of the tryptophan pathway enzymes. Three mutants, one of which contained a mutation that mapped within the
trpE
gene, were deficient in their ability to use glutamine as an amino donor in the formation of anthranilic acid. Another
trpE
mutation led to the production of an anthranilate synthetase with an increased sensitivity to feedback inhibition by tryptophan.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
14 articles.
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