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Query: UNIPROT:P06889 (Mol)
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Occurrence of a protein controlling urease synthesis (PIUS) at the transcriptional level in the lichen Evernia prunastri has been previously reported (Perez-Urria & Vicente, Physiol Plant 65: 433-438, 1985; id. Endocyt C Res 3: 311-316, 1986). In this work it was found that 0.1 mM cycloheximide seems to inhibit PIUS synthesis when lichen thalli are incubated on PIUS inducer, L-arginine. PIUS has been purified and characterized by PAGE, electrofocusing and amino acid analysis. It is a glycoprotein containing a homopolymer of fructose bound to the protein. PIUS has been located in whole thallus and lichenized mycobiont but remains undetectable in cultured fungi. PIUS is only detected in photobiont cells when they are axenically cultured on arginine. Thus, it is postulated that PIUS could be synthesized by lichenized photobionts from which it moves to mycobionts where it inhibits the production of fungal urease.
Plant Mol Biol 1989 Dec
PMID:Algal partner regulates fungal urease in the lichen Evernia prunastri by producing a protein which inhibits urease synthesis. 249 82

Intraperitoneal injections of urease induced a marked and sustained hyperammonemia in mice. Ultrastructural and stereologic analysis of hepatocytes from urease-treated mice showed striking changes in the mitochondria, rough and smooth endoplasmic reticulum and lysosomes. Thus, mitochondria became larger and rounder, and contained a less electron-dense matrix although their volume density remained similar to that of control cells. In addition, increases in the smooth and rough reticulum and the lysosomal compartment, were observed. Biochemical analysis of the livers from urease-treated mice revealed a significant increase in the intracellular content of water and lipids. Although the mechanism by which ammonia induces these changes remains unclear, the possible relationship between these findings and those described in the liver of humans and experimental animals in conditions of sustained hyperammonemia is discussed.
Virchows Arch B Cell Pathol Incl Mol Pathol 1984
PMID:Effects of urease-induced hyperammonemia in mouse liver. Ultrastructural, stereologic and biochemical study. 614

Arginine is rapidly depleted from the medium during the cultivation of T. vaginalis in a defined or semi-defined medium. It is broken down to ornithine, ammonia and carbon dioxide by the three enzymes of the dihydrolase pathway: arginine deiminase, catabolic ornithine carbamyltransferase (OCTase) and carbamate kinase. Arginase and urease as well as citrulline hydrolase appear to be absent. Ornithine, a product of the pathway was further converted to putrescine by an active ornithine decarboxylase. Apparent substrate Km values determined were arginine deiminase, 103 microM; catabolic OCTase, 71 microM; ornithine decarboxylase 134 microM. A substrate level phosphorylation is associated with the pathway; the significance of this to the overall energy economy of the cell is unclear.
Mol Biochem Parasitol 1983 Jul
PMID:The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis. 631 11

Urease activity is produced by members of the family Enterobacteriaceae that contain the plasmid-encoded urease locus only when urea is present in the growth medium. The plasmid-encoded urease locus contains seven tandem urease structural and accessory genes (ureDABCEFG). Previously we showed that transcription of the first gene in this cluster, ureD, is initiated at a urea-dependent promoter (ureDp). Expression from ureDp requires the product of ureR, which is transcribed divergently from the plasmid-encoded ureDABCEFG. From DNA sequence analysis, UreR is predicted to be a 34 kDa protein with identity to the AraC family of transcriptional activators. In this report we demonstrate that there are two additional urea and UreR-dependent promoters within the plasmid-encoded urease locus: ureRp and ureGp. A low-level constitutive promoter was also identified upstream of ureE (ureEp). Three major mRNA transcripts were induced when urea was present in the growth medium: a transcript containing ureDABCEF, a transcript corresponding to ureG, and a transcript corresponding to ureR. These results indicate that expression of each of the plasmid-encoded urease genes is transcriptionally regulated in response to urea and suggest that there is autogenous regulation of ureR. Therefore UreR is one of three AraC family members described thus far that are positively auto-regulated.
Mol Microbiol 1995 Apr
PMID:UreR activates transcription at multiple promoters within the plasmid-encoded urease locus of the Enterobacteriaceae. 765 Nov 32

Urease is a virulence determinant, a taxonomic and diagnostic marker, and immunogen for Helicobacter pylori, an aetiologic agent of gastritis and peptic ulceration. This enzyme requires Ni2+ ions in the active site for successful hydrolysis of urea. When expressed in Escherichia coli, recombinant urease is only weakly active unless urease structural subunits are overexpressed, exogenous NiCl2 is added, and the host strain is grown in medium that does not chelate free Ni2+. As wild-type H. pylori does not require such conditions for very high levels of urease expression, we reasoned that additional genes were required to accumulate the metal ion. To isolate such genes, E. coli SE5000 (pHP808), which carries the H. pylori urease gene cluster, was complemented with a lambda ZAP-derived plasmid library of the H. pylori chromosome. One of 1000 ampicillin-resistant clones, plated onto urea segregation agar, produced detectable urease. Urease activity of this co-transformant, grown in Luria broth containing 1 microM NiCl2, was 36 mumol NH3 min-1 mg-1 protein. Urease-enhancing activity, which is not directly linked to the urease gene cluster, was localized by subcloning and nucleotide sequencing. The largest open reading frame, designated nixA, predicted a polypeptide of 34,317 Da that displayed characteristics of an integral membrane protein. In vitro transcription-translation of nixA sequences yielded a polypeptide estimated to be 32 kDa in size. An in-frame Bal31 deletion within nixA abolished urease-enhancing activity. At 50 nM NiCl2, E. coli containing the nixA clone transported 1250 +/- 460 pmol Ni2+ min-1 10(-8) cells, whereas the vector control transported only 140 +/- 85 pmol Ni2+ min-1 10(8) cells, i.e. significantly less (P = 0.01). We conclude that NixA confers upon E. coli a high-affinity nickel-transport system (KT = 11.3 +/- 2.4 nM; Vmax = 1750 +/- 220 pmol Ni2+ min-1 10(-8) cells) and is necessary for expression of catalytically active urease, regardless of growth conditions.
Mol Microbiol 1995 Apr
PMID:Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. 765 Nov 42

All Helicobacter pylori isolates synthesize a 54 kDa immunodominant protein that was reported to be associated with the nickel-dependent urease of H. pylori. This protein was recently recognized as a homologue of the heat-shock protein of the GroEL class. The gene encoding the GroEL-like protein of H. pylori (HspB) was cloned (pILL689) and was shown to belong to a bicistronic operon including the hspA and hspB genes. In Escherichia coli, the constitutive expression of the hspA and hspB genes was initiated from a promoter located within an IS5 insertion element that mapped upstream to the two open reading frames (ORFs). IS5 was absent from the H. pylori genome, and was thus acquired during the cosmid cloning process. hspA and hspB encoded polypeptides of 118 and 545 amino acid residues, corresponding to calculated molecular masses of 13.0 and 58.2 kDa, respectively. Amino acid sequence comparison studies revealed that, although H. pylori HspA and HspB proteins were highly similar to their bacterial homologues, the H. pylori HspA featured a striking motif at the C-terminus. This unique motif consists of a series of cysteine and histidine residues resembling a nickel-binding domain, which is not present in any of the other bacterial GroES homologues so far characterized. When the pILL689 recombinant plasmid was introduced together with the H. pylori urease gene cluster (pILL763) into an E. coli host strain, an increase of urease activity was observed. This suggested a close interaction between the HspA and HspB proteins and the urease enzyme, and a possible role for HspA in the chelation of nickel ions. The genes encoding each of the HspA and HspB polypeptides were cloned, expressed independently as proteins fused to the maltose-binding protein (MBP) and purified in large scale. The MBP-HspA and MBP-HspB fusion proteins were shown to retain their antigenic properties. Both HspA and HspB represent antigens that are specifically recognized by the sera from H. pylori-infected patients. Whereas HspB was known to be immunogenic in humans, this is the first demonstration that HspA per se is also immunogenic.
Mol Microbiol 1994 Dec
PMID:Helicobacter pylori hspA-hspB heat-shock gene cluster: nucleotide sequence, expression, putative function and immunogenicity. 771 57

We sought to determine the genetic basis of expression of the ubiquitous (metabolic) urease of soybean. This isozyme is termed the metabolic urease because its loss, in eu4/eu4 mutants, leads to accumulation of urea, whereas loss of the embryo-specific urease isozyme does not. The eu4 lesion eliminated the expression of the ubiquitous urease in vegetative and embryonic tissues. RFLP analysis placed urease clone LC4 near, or within, the Eu4 locus. Sequence comparison of urease proteins (ubiquitous and embryo-specific) and clones (LC4 and LS1) indicated that LC4 and LS1 encode ubiquitous and embryo-specific ureases, respectively. That LC4 is transcribed into poly(A)+ RNA in all tissues was indicated by the amplification of its transcript by an LC4-specific PCR primer. (The LS1-specific primer, on the other hand, amplified poly(A)+ RNA only from developing embryos expressing the embryo-specific urease.) These observations are consistent with Eu4 being the ubiquitous urease structural gene contained in the LC4 clone. In agreement with this notion, the mutant phenotype of eu4/eu4 callus was partially corrected by the LC4 urease gene introduced by particle bombardment.
Mol Gen Genet 1994 Feb
PMID:A single gene (Eu4) encodes the tissue-ubiquitous urease of soybean. 790 65

The nickel metalloenzyme urease catalyses the hydrolysis of urea to ammonia and carbamate, and thus generates the preferred nitrogen source of many organisms. When produced by bacterial pathogens in either the urinary tract or the gastroduodenal region, urease acts as a virulence factor. At both sites of infection urease is known to enhance the survival of the infecting bacteria. Ammonia resulting from the action of urease is believed to increase the pH of the environment to one more favourable for growth, and to injure the surrounding epithelial cells. In addition, in the urinary tract urease activity can result in the formation of urinary calculi. Bacterial urease gene clusters contain from seven to nine genes depending upon the species. These genes encode the urease structural subunits and accessory polypeptides involved in the biosynthesis of the nickel metallocentre. So far, three distinct mechanisms of urease gene expression have been described for ureolytic bacteria. Some species constitutively produce urease; some species produce urease only if urea is present in the growth medium; and some species produce urease only during nitrogen-limiting growth conditions. For either the urea-inducible genes or the nitrogen-regulated genes transcription appears to be positively regulated. In the nitrogen-regulated systems, urease gene expression requires Nac (nitrogen assimilation control), a member of the LysR family of transcriptional activators. Urea dependent expression of urease requires UreR (urease regulator), a member of the AraC family of transcriptional activators. An evolutionary tree for urease genes of eight bacterial species is proposed.
Mol Microbiol 1993 Sep
PMID:Bacterial ureases: structure, regulation of expression and role in pathogenesis. 793 18

The genes encoding urease were cloned from Bordetella bronchiseptica and the 5.2 kb of DNA essential for expression analysed in a T7 RNA polymerase transcription-translation system. At least four polypeptides with predicted molecular weights of 69,000, 26,000, 12,200 and 11,000 were found. Partial DNA sequence of the gene encoding the 69,000 Da polypeptide revealed high amino acid identity to the alpha-subunit of Proteus mirabilis urease, UreC and jack bean urease. A stable, unmarked deletion was constructed in this gene to create a urease-negative mutant of B. bronchiseptica. To assess colonization in a guinea-pig model, the urease-negative strain was inoculated with the urease-positive parental strain in a mixed infection. The urease-negative strain out competed the urease-positive strain in the trachea, lungs and caecum. We demonstrate that urease is not essential for B. bronchiseptica colonization of the guinea-pig respiratory and digestive tracts.
Mol Microbiol 1993 Nov
PMID:Cloning of Bordetella bronchiseptica urease genes and analysis of colonization by a urease-negative mutant strain in a guinea-pig model. 796 32

Yersinia enterocolitica is a facultative intracellular parasite, displaying the ability to grow saprophytically or invade and persist intracellularly in the mammalian reticuloendothelial system. The transition between such diverse environments requires the co-ordinated regulation of specific sets of genes on both the chromosome and virulence plasmid. Temperature has a profound pleiotropic effect on gene expression and phenotypically promotes alterations in cell morphology, outer-membrane protein synthesis, urease production, lipopolysaccharide synthesis, motility, and synthesis of genes involved in invasion of eukaryotic host cells. By examining thermoregulated flagella biosynthesis, we have determined that motility is repressed at 25 degrees C (permissive temperature) with subinhibitory concentrations of novobiocin. These conditions also induce virulence gene expression suggesting novobiocin addition simulates, at least partially, a high-temperature environment. Furthermore, temperature-shift experiments, using Y. enterocolitica containing pACYC184 as a reporter plasmid, indicate that thermo-induced alterations of DNA supercoiling coincide with temperature-induced phenotypic changes. A class of putative DNA gyrase mutant (novobiocin resistant) likewise demonstrates the 37 degrees C phenotype when cultured at 25 degrees C; it is non-motile, urease negative, calcium growth dependent, and positive for Yop expression. These results support a model implicating DNA topology as a contributing factor of Y. enterocolitica thermoregulation.
Mol Microbiol 1994 Apr
PMID:Thermoregulation in Yersinia enterocolitica is coincident with changes in DNA supercoiling. 805 44


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