Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.13.3 (histidine kinase)
 2,405 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have previously reported the identification of two genes, pilA and pilB, which act in trans to regulate pilus expression in Neisseria gonorrhoeae. Here we show that PilA and PilB have amino acid sequence similarities with members of the two component 'sensor-regulator' family of proteins. PilB has homology with histidine kinase sensors. Alkaline phosphatase fusions to the predicted sensor and transmitter domains are described. Their PhoA activity and cellular location suggest that PilB is inserted in the cytoplasmic membrane and predict periplasmic and cytoplasmic locations for the sensor and the transmitter domains, respectively. PilA has homology with response regulators in its N-terminal part, and with components of the eukaryotic protein secretory apparatus (SRP 54 and SRP receptor) as well as two Escherichia coli gene products in its C-terminal part. In particular, it contains a putative GTP-binding site. Mini-transposon insertions into different regions of pilA were obtained. The phenotypes and genotypes of these mutants and preliminary biochemical studies of the gene products of two of these mutants lend further support to the hypothesis that PilA is a DNA-binding response regulator and confirm that it participates in an essential function in the bacterium.
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PMID:Control of pilus expression in Neisseria gonorrhoeae as an original system in the family of two-component regulators. 184 4

Of the numerous two-component signal transduction systems found in bacteria, only a very few have proven to be essential for cell viability. Among these is the YycF (response regulator)-YycG (histidine kinase) system, which is highly conserved in and specific to the low-G+C content gram-positive bacteria. Given the pathogenic nature of several members of this class of bacteria, the YycF-YycG system has been suggested as a prime antimicrobial target. In an attempt to identify genes involved in regulation of this two-component system, a transposon mutagenesis study was designed to identify suppressors of a temperature-sensitive YycF mutant in Bacillus subtilis. Suppressors could be identified, and the prime target was the yycH gene located adjacent to yycG and within the same operon. A lacZ reporter assay revealed that YycF-regulated gene expression was elevated in a yycH strain, whereas disruption of any of the three downstream genes within the operon, yycI, yycJ, and yycK, showed no such effect. The concentrations of both YycG and YycF, assayed immunologically, remained unchanged between the wild-type and the yycH strain as determined by immunoassay. Alkaline phosphatase fusion studies showed that YycH is located external to the cell membrane, suggesting that it acts in the regulation of the sensor domain of the YycG sensor histidine kinase. The yycH strain showed a characteristic cell wall defect consistent with the previously suggested notion that the YycF-YycG system is involved in regulating cell wall homeostasis and indicating that either up- or down-regulation of YycF activity affects this homeostatic mechanism.
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PMID:YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis. 1603 Feb 36

In Synechocystis sp. PCC 6803 extracellular phosphate levels are relayed to the pho regulon via the SphS histidine kinase. In this cyanobacterium, the start codon of sphS has been assigned as a GUG, thereby predicting SphS to be a cytosolic protein lacking a putative N-terminal region found in the PhoR orthologue from Escherichia coli. Inspection upstream of sphS located an in-frame AUG positioned 47 codons in front of the putative GUG start. Alterations at either of the putative AUG or GUG start codons did not prevent transcription of sphS; however, up-regulation of alkaline phosphatase mRNA, or alkaline phosphatase activity, was not detected in response to phosphate-limiting conditions when the AUG was mutated. Alkaline phosphatase expression and activity serve as phenotypic markers for activation of the pho regulon. Therefore, the pho regulon had not been induced in these cells, whereas normal up-regulation was observed in strains carrying mutations at the GUG. These results show that the AUG codon, not the GUG codon, is the initiation site for sphS translation in Synechocystis sp. PCC 6803.
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PMID:Identification of the start codon for sphS encoding the phosphate-sensing histidine kinase in Synechocystis sp. PCC 6803. 1757 13