Disease relevance of hisJ

• The hisJ and argT genes of Salmonella typhimurium encode two periplasmic binding proteins, J and LAO, which are involved in histidine and arginine transport, respectively, and which interact with a common membrane-bound component, the P protein [1].
• The three promoters are the argTr (arginine transport) and dhuA (histidine transport) promoters of Salmonella typhimurium and the nifH (nitrogenase) promoter of Rhizobium meliloti [2].
• Five independently isolated promoter-up mutations were transferred to an M13 hybrid phage that carries the histidine transport operon, and their nucleotide sequences were determined [3].
• Cloning of the histidine transport genes from Salmonella typhimurium and characterization of an analogous transport system in Escherichia coli [4].

High impact information on hisJ

• Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium [5].
• Proteoliposomes do not catalyze significant ATP hydrolysis until histidine transport is initiated by addition of substrate along with HisJ, the water-soluble histidine-binding protein [6].
• We have determined the nucleotide sequences of the regulatory regions from two amino acid transport operons from Salmonella typhimurium: dhuA, which regulates the histidine transport operon, and argTr, which regulates argT, the gene encoding the lysine-arginine-ornithine-binding protein, LAO [7].
• The promoter for the histidine transport operon has been identified from the sequence change in the promoter-up mutation dhuA1 [7].
• The P protein was shown previously by genetic analysis to interact with the periplasmic histidine-binding protein J, another essential component of histidine transport [8].

Chemical compound and disease context of hisJ

• The periplasmic histidine-binding protein, HisJ, and the lysine-, arginine-, ornithine-binding protein (LAO) are receptors for histidine transport via the histidine permease of Salmonella typhimurium [9].

Biological context of hisJ

• The results indicate that intra-operonic regulation is due to a combination of factors including efficiency of translational initiation, mRNA degradation, and retroregulation of hisJ expression [10].
• The F' factors carry an intact dhuA hisJ portion of the histidine transport operon [11].
• The hisJ-generated amplicons from six culture-negative and six culture-positive specimens were sequenced and analyzed using DNA sequence alignment and phylogenetic analysis software [12].
• A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis [13].
• Afine-structure genetic map of the histidine transport region of the Salmonella typhimurium chromosome was constructed [14].

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

• The Salmonella typhimurium periplasmic histidine-binding J-protein is one of four proteins encoded by the histidine transport operon [17].

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].

References