Location of the gene for the low-affinity tryptophan-specific permease of Escherichia coli

Abstract

L-Tryptophan uptake was assayed under conditions in which the aroT gene had been inactivated by deletion and r354w2.r356w1 =1,2-Di-O-acyl-3-O-(6-(3(2)-D-alanyl-sn-glycerol-1-phospho) -β-D-glucopyranosyl(1-6)-β-D-glucopyrasonyl)-glycerol the product of the aroP permease was competitively inhibited. 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 λtna+.