Abstract
L-Tryptophan uptake was assayed under conditions in which the aroT gene had been inactivated by deletion and the product of the aroP permease was competitively inhibition. A mutant carrying a deletion from bgl through tnaA showed negligible L-tryptophan uptake, in contrast to a strain possessing an intact tna region or to strains carrying point mutations in tna. The ability to take up L-tryptophan was not restored by lysogenizing the tna-deleted strain with lambda tna+.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Transport Systems*
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins*
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Genes, Bacterial*
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Lysogeny
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Membrane Transport Proteins / genetics*
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Mutation
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Saccharomyces cerevisiae Proteins*
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Tryptophan / metabolism
Substances
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Amino Acid Transport Systems
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Escherichia coli Proteins
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Membrane Transport Proteins
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Saccharomyces cerevisiae Proteins
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TAT2 protein, S cerevisiae
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TnaB protein, E coli
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Tryptophan