Genetic and Biochemical Studies of Transport Systems for Branched-chain Amino Acids in Escherichia Coli

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1979 Apr 1

PMID 374366

Citations 12

Authors

I Yamato

M Ohki

Y Anraku

Affiliations

Soon will be listed here.

Abstract

Mutants of Escherichia coli K-12 requiring high concentrations of branched-chain amino acids for growth were isolated. One of the mutants was shown to be defective in transport activity for branched-chain amino acids. The locus of the mutation (hrbA) was mapped at 8.9 min on the E. coli genetic map by conjugational and transductional crosses. The gene order of this region is proC-hrbA-tsx. The hrbA system was responsible for the uptake activity of cytoplasmic membrane vesicles. It was not repressed by leucine. The substrate specificities and kinetics of the uptake activities were studied using cytoplasmic membrane vesicles and intact cells of the mutants grown in the presence or absence of leucine. Results showed that there are three transport systems for branched-chain amino acids, LIV-1, -2, and -3. The LIV-2 and -3 transport systems are low-affinity systems, the activities of which are detectable in cytoplasmic membrane vesicles. The systems are inhibited by norleucine but not by threonine. The LIV-2 system is also repressed by leucine. The LIV-1 transport system is a high-affinity system that is sensitive to osmotic shock. When the leucine-isoleucine-valine-threonine-binding protein is derepressed, the high-affinity system can be inhibited by threonine.

Citing Articles

Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12.

Koyanagi T, Katayama T, Suzuki H, Kumagai H J Bacteriol. 2004; 186(2):343-50.

PMID: 14702302 PMC: 305776. DOI: 10.1128/JB.186.2.343-350.2004.

Cloning and nucleotide sequencing of a Staphylococcus aureus gene encoding a branched-chain-amino-acid transporter.

Vijaranakul U, Xiong A, Lockwood K, Jayaswal R Appl Environ Microbiol. 1998; 64(2):763-7.

PMID: 9464420 PMC: 106115. DOI: 10.1128/AEM.64.2.763-767.1998.

Cloning and characterization of brnQ, a gene encoding a low-affinity, branched-chain amino acid carrier in Lactobacillus delbrückii subsp. lactis DSM7290.

Stucky K, Hagting A, Klein J, Matern H, Henrich B, Konings W Mol Gen Genet. 1995; 249(6):682-90.

PMID: 8544834 DOI: 10.1007/BF00418038.

Functions of the gene products of Escherichia coli.

Riley M Microbiol Rev. 1993; 57(4):862-952.

PMID: 7508076 PMC: 372942. DOI: 10.1128/mr.57.4.862-952.1993.

Genetic and biochemical studies of transport systems for branched-chain amino acids in Escherichia coli K-12: isolation and properties of mutants defective in leucine-repressible transport activities.

Yamato I, Anraku Y J Bacteriol. 1980; 144(1):36-44.

PMID: 6998958 PMC: 294582. DOI: 10.1128/jb.144.1.36-44.1980.

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