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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

hisJ  -  histidine ABC transporter substrate...

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

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Disease relevance of hisJ


High impact information on hisJ


Chemical compound and disease context of hisJ


Biological context of hisJ


Associations of hisJ with chemical compounds

  • A mutant J protein, with a defective interaction site but intact histidine-binding site, can function in histidine transport if an appropriate compensating mutation is introduced in the P protein [15].
  • Possible mechanism for the interaction of the J, P, and Q components in histidine transport, and of P and Q in lysine/arginine/ornithine transport, are discussed [8].
  • We established that in both bacterial species these genes were cotransducible with the neighboring histidine transport operon and were distally located relative to purF. pta mutants were sensitive to the dye alizarin yellow and were unable to grow on medium containing inositol as a carbon source [16].

Physical interactions of hisJ


Other interactions of hisJ

  • The level of expression of hisJ is 30-fold greater than that of hisP [10].
  • They also suggest that the REP (Repetitive Extragenic Palindromic) sequences, which are located in the hisJ-hisQ intercistronic region, may interfere with translation of the hisQ gene and affect upstream messenger RNA stability by protecting it from 3' to 5' nuclease degradation (in agreement with data presented by Newbury et al., 1987) [10].
  • The orientation of this operon relative to purF has been established by three-point crosses as being: purF duhA hisJ hisP [14].
  • 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 [18].
  • The lrp mutations arise as suppressors of mutations in the genes encoding the histidine permease which drastically decrease the level of histidine transport activity [19].

Analytical, diagnostic and therapeutic context of hisJ

  • PCR detection of Salmonella spp. using the hisJ primers and the invE-A primers had a sensitivity of 93.3 and 80%, respectively, and a specificity of 85.6 and 98.6%, respectively, compared with bacterial culture [12].


  1. Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences. Higgins, C.F., Ames, G.F. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  2. Promoters regulated by the glnG (ntrC) and nifA gene products share a heptameric consensus sequence in the -15 region. Ow, D.W., Sundaresan, V., Rothstein, D.M., Brown, S.E., Ausubel, F.M. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  3. Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing. Lee, G.S., Ames, G.F. J. Bacteriol. (1984) [Pubmed]
  4. Cloning of the histidine transport genes from Salmonella typhimurium and characterization of an analogous transport system in Escherichia coli. Ardeshir, F., Ames, G.F. J. Supramol. Struct. (1980) [Pubmed]
  5. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Higgins, C.F., Haag, P.D., Nikaido, K., Ardeshir, F., Garcia, G., Ames, G.F. Nature (1982) [Pubmed]
  6. Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport. Bishop, L., Agbayani, R., Ambudkar, S.V., Maloney, P.C., Ames, G.F. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  7. Regulatory regions of two transport operons under nitrogen control: nucleotide sequences. Higgins, C.F., Ames, G.F. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  8. Identification of a membrane protein as a histidine transport component in Salmonella typhimurium. Ames, G.F., Nikaido, K. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  9. The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies. Wolf, A., Shaw, E.W., Nikaido, K., Ames, G.F. J. Biol. Chem. (1994) [Pubmed]
  10. Role of the intercistronic region in post-transcriptional control of gene expression in the histidine transport operon of Salmonella typhimurium: involvement of REP sequences. Stern, M.J., Prossnitz, E., Ames, G.F. Mol. Microbiol. (1988) [Pubmed]
  11. Isolation of F' plasmids carrying a portion of the Salmonella typhimurium histidine transport operon. Lawton, K.G., Taber, H.W. J. Bacteriol. (1984) [Pubmed]
  12. Identification of two phylogenetically related organisms from feces by PCR for detection of Salmonella spp. Gentry-Weeks, C., Hutcheson, H.J., Kim, L.M., Bolte, D., Traub-Dargatz, J., Morley, P., Powers, B., Jessen, M. J. Clin. Microbiol. (2002) [Pubmed]
  13. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Noel, D., Nikaido, K., Ames, G.F. Biochemistry (1979) [Pubmed]
  14. Fine-structure map of the histidine transport genes in Salmonella typhimurium. Ames, G.F., Noel, K.D., Taber, H., Spudich, E.N., Nikaido, K., Afong, J. J. Bacteriol. (1977) [Pubmed]
  15. Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein. Ames, G.F., Spurich, E.N. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  16. Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella typhimurium. LeVine, S.M., Ardeshir, F., Ames, G.F. J. Bacteriol. (1980) [Pubmed]
  17. Conformational dynamics of two histidine-binding proteins of Salmonella typhimurium. Zukin, R.S., Klos, M.F., Hirsch, R.E. Biophys. J. (1986) [Pubmed]
  18. 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. Payne, G.M., Spudich, E.N., Ames, G.F. Mol. Gen. Genet. (1985) [Pubmed]
  19. D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp). Hecht, K., Zhang, S., Klopotowski, T., Ames, G.F. J. Bacteriol. (1996) [Pubmed]
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