Abstract
A new class of D-histidine-utilizing mutants which carry mutations in the gene encoding the leucine-responsive regulatory protein (Lrp) has been identified in Salmonella typhimurium. The lrp mutations arise as suppressors of mutations in the genes encoding the histidine permease which drastically decrease the level of histidine transport activity. However, the suppressor effect is not exerted by elevating the level of the permease. Rather, the properties of the suppressor mutants are consistent with the notion that the parent permease mutants transport D-histidine at a low level and that in the suppressor mutants D-histidine is utilized effectively through elevated levels of racemization. The enzymatic activity of D-alanine dehydrogenase (Dad) is shown to be elevated in the suppressor mutants and is a possible pathway of D-histidine utilization. The suppressor mutations are located in the helix-turn-helix region of Lrp.
MeSH Terms
ATP-Binding Cassette Transporters
Alanine Dehydrogenase
Amino Acid Oxidoreductases/metabolism
Amino Acid Transport Systems, Basic
Bacterial Proteins/genetics,physiology
Biological Transport
DNA-Binding Proteins/genetics,physiology
Genes, Bacterial/genetics
Genes, Suppressor/physiology
Helix-Turn-Helix Motifs
Histidine/metabolism
Leucine-Responsive Regulatory Protein
Membrane Transport Proteins/genetics
Mutation
Salmonella typhimurium/genetics,metabolism
Stereoisomerism
Transcription Factors
Chemicals
ATP-Binding Cassette Transporters
Amino Acid Transport Systems, Basic
Bacterial Proteins
DNA-Binding Proteins
Membrane Transport Proteins
Transcription Factors
Leucine-Responsive Regulatory Protein
Histidine
histidine permease, Bacteria
Amino Acid Oxidoreductases
Alanine Dehydrogenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hecht K
Department of Molecular and Cell Biology, University of California at Berkeley 94720, USA.
Zhang S
Klopotowski T
Ames G F
References (24)
24 references, click to expand
-
A mutational hot-spot in the hisM gene of the histidine transport operon in Salmonella typhimurium is due to deletion of repeated sequences and results in an altered specificity of transport.
Mol Gen Genet. 1985;200(3):493-6
PMID: 3900641
-
Bacterial periplasmic transport systems: structure, mechanism, and evolution.
Annu Rev Biochem. 1986;55:397-425
PMID: 3527048
-
Genetic analysis in Salmonella typhimurium with a small collection of randomly spaced insertions of transposon Tn10 delta 16 delta 17.
J Bacteriol. 1987 May;169(5):1787-93
PMID: 3032894
-
Improved detection of helix-turn-helix DNA-binding motifs in protein sequences.
Nucleic Acids Res. 1990 Sep 11;18(17):5019-26
PMID: 2402433
-
Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine.
J Bacteriol. 1993 Feb;175(4):1110-7
PMID: 8432705
-
The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies.
J Biol Chem. 1994 Sep 16;269(37):23051-8
PMID: 7521874
-
The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli.
Microbiol Rev. 1994 Sep;58(3):466-90
PMID: 7968922
-
The amino acid sequence of Lrp is highly conserved in four enteric microorganisms.
J Bacteriol. 1995 Mar;177(6):1624-6
PMID: 7883720
-
Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form.
J Biol Chem. 1995 Jul 7;270(27):16097-106
PMID: 7608172
-
Leucine-responsive regulatory protein: a global regulator of gene expression in E. coli.
Annu Rev Microbiol. 1995;49:747-75
PMID: 8561478
-
UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM.
Arch Biochem Biophys. 1964 Jan;104:1-18
PMID: 14110716
-
Mutants of Salmonella typhimurium able to utilize D-histidine as a source of L-histidine.
J Bacteriol. 1971 Jan;105(1):28-37
PMID: 5541014
-
The histidine-binding protein J is a component of histidine transport. Identification of its structural gene, hisJ.
J Biol Chem. 1972 Jul 10;247(13):4309-16
PMID: 4556307
-
Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions.
J Biol Chem. 1974 Jan 25;249(2):634-44
PMID: 4129205
-
D-amino acid dehydrogenase: the enzyme of the first step of D-histidine and D-methionine racemization in Salmonella typhimurium.
Mol Gen Genet. 1974;128(2):131-46
PMID: 4150767
-
The histidine-binding protein J, a histidine transport component, has two different functional sites.
J Biol Chem. 1974 Nov 10;249(21):6976-83
PMID: 4213931
-
Mapping of two loci affecting the regulation of branched-chain amino acid transport in Escherichia coli K-12.
J Bacteriol. 1976 Apr;126(1):80-90
PMID: 770444
-
Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein.
Proc Natl Acad Sci U S A. 1976 Jun;73(6):1877-81
PMID: 778848
-
Fine-structure map of the histidine transport genes in Salmonella typhimurium.
J Bacteriol. 1977 Mar;129(3):1289-97
PMID: 321422
-
Duplications of histidine transport genes in Salmonella typhimurium and their use for the selection of deletion mutants.
J Bacteriol. 1978 Dec;136(3):1094-108
PMID: 363688
-
Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems.
J Bacteriol. 1979 Apr;138(1):218-34
PMID: 35521
-
D-Amino acid dehydrogenase of Escherichia coli K12: positive selection of mutants defective in enzyme activity and localization of the structural gene.
Mol Gen Genet. 1981;181(3):373-8
PMID: 6113535
-
Two alanine racemase genes in Salmonella typhimurium that differ in structure and function.
J Bacteriol. 1983 Mar;153(3):1439-50
PMID: 6298185
-
Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing.
J Bacteriol. 1984 Sep;159(3):1000-5
PMID: 6090381