D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp)

Journal of Bacteriology

Volumn 178, Issue 2, 1996, Pages 327-331

  Hecht, Katrin ^a,c   Zhang, Sue ^a   Klopotowski, Tadeusz ^b   Ames, Giovanna Ferro Luzzi ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^c F60   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE DEHYDROGENASE; HISTIDINE; REGULATOR PROTEIN;

AMINO ACID METABOLISM; AMINO ACID TRANSPORT; ARTICLE; BACTERIAL GENE; BACTERIUM MUTANT; CONTROLLED STUDY; GENE REPRESSION; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM;

BACTERIA (MICROORGANISMS); SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0029671287     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.2.327-331.1996     Document Type: Article

References (26)

1. Ames, G. F.-L. 1964. Uptake of amino acids by Salmonella typhimurium. Arch. Biochem. Biophys. 104:1-18.
2. Ames, G. F.-L. 1974. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs, membrane, soluble, and periplasmic fractions. J. Biol. Chem. 249:634-644.
3. Ames, G. F.-L. 1986. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 55:397-425.
4. Ames, G. F.-L., D. P. Biek, and E. N. Spudich. 1978 Duplications of histidine transport genes in S typhimurium and their use for the selection of deletion mutants. J. Bacteriol. 136:1094-1108.
5. Ames, G. F.-L., and J. E. Lever. 1972. The histidine-binding protein J is a component of histidine transport: identification of its structural gene, hisJ. J. Biol. Chem. 247:4309-4316.
6. Ames, G. F.-L., K. D. Noel, H. Taber, E. N. Spudich, K. Nikaido, J. Afong, and F. Ardeshir. 1977. Fine-structure map of the histidine transport genes in Salmonella typhimurium. J. Bacteriol. 129:1289-1297.
7. Ames, G. F.-L., and E. N. Spudich. 1976. Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein Proc. Natl Acad. Sci. USA 73:1877-1881
8. Anderson, J. J., S. C. Quay, and D. L. Oxender. 1976 Mapping of two loci affecting the regulation of branched-chain amino acid transport in Escherichia coli K-12 J. Bacteriol. 126:80-90.
9. Calvo, J. M., and R. G. Matthews. 1994. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol. Rev 58:466-490.
10. Dodd, I. B., and J. B. Egan. 1990. Improved detection of helix-turn-helix DNA-binding motifs in protein sequences. Nucleic Acids Res. 18:5019-5026
11. Freundlich, M., and E. Mathew. Personal communication.
12. Friedberg, D., J. V. Platko, B. Tyler, and J. M. Calvo. 1995 The amino acid sequence of Lrp is highly conserved in four enteric microorganisms. J. Bacteriol. 177:1624-1626
13. Krajewska-Grynkiewicz, K., W. Walczak, and T. Klopotowski. 1971. Mutants of Salmonella typhimurium able to utilize D-histidine as a source of L-histidine. J. Bacteriol. 105:28-37
14. Kukral, A. M., K. L. Strauch, R. A. Maurer, and C. G. Miller. 1987. Genetic analysis of Salmonella typhimurium with a small collection of randomly spaced insertions of transposon Tn10Δ16Δ17. J Bacteriol. 169:1787-1793.
15. Kustu, S. G., and G. F.-L. Ames. 1974. The histidine-binding protein J, a histidine transport component, has two different functional sites. J. Biol. Chem. 249:6976-6983.
16. Kustu, S. G., N. C. McFarland, S. P. Hui, B. Esmon, and G. F.-L. Ames. 1979. Nitrogen control in Salmonella typhimurium: coregulation of synthesis of glutamine synthetase and amino acid transport systems. J. Bacteriol. 138:218-234.
17. Lee, G. S., and G. F.-L. Ames. 1984. Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing. J. Bacteriol. 159:1000-1005
18. Newman, E. B., and R. Lin. 1995. Leucine-responsive regulatory protein: a global regulator of gene expression in E coli 49:747-775.
19. Payne, G., E. N. Spudich, and G. F.-L. Antes. 1985 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. 200:493-496.
20. Platko, J. V., and J. M. Calvo. 1993. Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine. J. Bacteriol. 175:1110-1117
21. Roth, J. R. 1970. Genetic techniques in studies of bacterial metabolism. Methods Enzymol. 17A:3-35.
22. Wasserman, S. A., C. T. Walsh, and D. Botstein. 1983 Two alanine racemase genes in Salmonella typhimurium that differ in structure and function J Bacteriol. 153:1439-1450.
23. Wild, J., and T. Klopotowski. 1981. 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 181:373-378.
24. Wild, J., W. Walczac, K. Krajewska-Grynkiewicz, and T. Klopotowski. 1974. D-Amino acid dehydrogenase: the enzyme of the first step of D-histidine and D-methionine racemization in Salmonella typhimurium. Mol Gen Genet. 128:131-146.
25. Wolf, A., E. W. Shaw, K. Nikaido, and G. F.-L. Ames. 1994. The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies. J. Biol. Chem. 269:23051-23058.
26. Wolf, A., E. W. Shaw, B.-H. Oh, H. De Bondt, A. K. Joshi, and G. F.-L. Ames. 1995. 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. 270:16097-16106.