Academic literature on the topic 'Bacterial urea transport'
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Journal articles on the topic "Bacterial urea transport"
1
Godara, Geeta, Craig Smith, Janine Bosse, Mark Zeidel, and John Mathai. "Functional characterization ofActinobacillus pleuropneumoniaeurea transport protein, ApUT." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 296, no. 4 (April 2009): R1268—R1273. http://dx.doi.org/10.1152/ajpregu.90726.2008.
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Urea transporters (UTs) effect rapid flux of urea across biological membranes. In the mammalian kidney, UT activity is essential for effective urine concentration. In bacteria, UT-mediated urea uptake permits intracellular urease to degrade urea to ammonia and CO2, a process that either buffers acid loads or provides nutrient nitrogen. We have characterized the urea transport channel protein ApUT from Actinobacillus pleuropneumoniae. Kinetic analysis of bacterial inside-out membranes enriched in ApUT showed ∼28-fold increase in urea permeability (3.3 ± 0.4 × 10−4cm/s) compared with control vesicles (0.11 ± 0.02 × 10−4cm/s). In addition to urea, ApUT also conducts water. Urea and water transport across the channel was phloretin and mercury inhibitable, and the site of inhibition may be located on the cytoplasmic side of the protein. Glycerol and urea analogs, such as methylamine, dimethylurea, formamide, acetamide, methylurea, propanamide, and ethylamine did not permeate across ApUT.
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Scott, David R., Elizabeth A. Marcus, Yi Wen, Siddarth Singh, Jing Feng, and George Sachs. "Cytoplasmic Histidine Kinase (HP0244)-Regulated Assembly of Urease with UreI, a Channel for Urea and Its Metabolites, CO2, NH3, and NH4+, Is Necessary for Acid Survival of Helicobacter pylori." Journal of Bacteriology 192, no. 1 (October 23, 2009): 94–103. http://dx.doi.org/10.1128/jb.00848-09.
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ABSTRACT Helicobacter pylori colonizes the normal human stomach by maintaining both periplasmic and cytoplasmic pH close to neutral in the presence of gastric acidity. Urease activity, urea flux through the pH-gated urea channel, UreI, and periplasmic α-carbonic anhydrase are essential for colonization. Exposure to pH 4.5 for up to 180 min activates total bacterial urease threefold. Within 30 min at pH 4.5, the urease structural subunits, UreA and UreB, and the Ni2+ insertion protein, UreE, are recruited to UreI at the inner membrane. Formation of this complex and urease activation depend on expression of the cytoplasmic sensor histidine kinase, HP0244. Its deletion abolishes urease activation and assembly, impairs cytoplasmic and periplasmic pH homeostasis, and depolarizes the cells, with an ∼7-log loss of survival at pH 2.5, even in 10 mM urea. Associated with this assembly, UreI is able to transport NH3, NH4 +, and CO2, as shown by changes in cytoplasmic pH following exposure to NH4Cl or CO2. To be able to colonize cells in the presence of the highly variable pH of the stomach, the organism expresses two pH-sensor histidine kinases, one, HP0165, responding to a moderate fall in periplasmic pH and the other, HP0244, responding to cytoplasmic acidification at a more acidic medium pH. Assembly of a pH-regulatory complex of active urease with UreI provides an advantage for periplasmic buffering.
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Hong, Wu, Kouichi Sano, Shinichi Morimatsu, David R. Scott, David L. Weeks, George Sachs, Toshiyuki Goto, et al. "Medium pH-dependent redistribution of the urease of Helicobacter pylori." Journal of Medical Microbiology 52, no. 3 (March 1, 2003): 211–16. http://dx.doi.org/10.1099/jmm.0.05072-0.
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Helicobacter pylori is an aetiological agent of gastric disease. Although the role of urease in gastric colonization of H. pylori has been shown, it remains unclear as to where urease is located in this bacterial cell. The purpose of this study was to define the urease-associated apparatus in the H. pylori cytoplasm. H. pylori was incubated at both a neutral and an acidic pH in the presence or absence of urea and examined by double indirect immunoelectron microscopy. The density of gold particles for UreA was greatest in the inner portion of the wild-type H. pylori cytoplasm at neutral pH but was greatest in the outer portion at acidic pH. This difference was independent of the presence of urea and was not observed in the ureI-deletion mutant. Also, the eccentric shift of urease in acidic pH was not observed in UreI. After a 2 day incubation period at acidic pH, it was observed that the urease gold particles in H. pylori assembled and were associated with UreI gold particles. Urease immunoreactivity shifted from the inner to the outer portion of H. pylori as a result of an extracellular decrease in pH. This shift was urea-independent and UreI-dependent, suggesting an additional role of UreI in urease-dependent acid resistance. This is the first report of the intracellular transport of molecules in bacteria in response to changes in the extracellular environment.
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Rodela, T. M., J. S. Ballantyne, and P. A. Wright. "Carrier-mediated urea transport across the mitochondrial membrane of an elasmobranch (Raja erinacea) and a teleost (Oncorhynchus mykiss) fish." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 294, no. 6 (June 2008): R1947—R1957. http://dx.doi.org/10.1152/ajpregu.00251.2007.
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In osmoregulating teleost fish, urea is a minor nitrogen excretory product, whereas in osmoconforming marine elasmobranchs it serves as the major tissue organic solute and is retained at relatively high concentrations (∼400 mmol/l). We tested the hypothesis that urea transport across liver mitochondria is carrier mediated in both teleost and elasmobranch fishes. Intact liver mitochondria in rainbow trout ( Oncorhynchus mykiss) demonstrated two components of urea uptake, a linear component at high concentrations and a phloretin-sensitive saturable component [Michaelis constant ( Km) = 0.58 mmol/l; maximal velocity ( Vmax) = 0.12 μmol·h−1·mg protein−1] at lower urea concentrations (<5 mmol/l). Similarly, analysis of urea uptake in mitochondria from the little skate ( Raja erinacea) revealed a phloretin-sensitive saturable transport ( Km= 0.34 mmol/l; Vmax= 0.054 μmol·h−1·mg protein−1) at low urea concentrations (<5 mmol/l). Surprisingly, urea transport in skate, but not trout, was sensitive to a variety of classic ionophores and respiration inhibitors, suggesting cation sensitivity. Hence, urea transport was measured in the reverse direction using submitochondrial particles in skate. Transport kinetics, inhibitor response, and pH sensitivity were very similar in skate submitochondrial particle submitochondrial particles ( Km= 0.65 mmol/l, Vmax= 0.058 μmol·h−1·mg protein−1) relative to intact mitochondria. We conclude that urea influx and efflux in skate mitochondria is dependent, in part, on a bidirectional proton-sensitive mechanism similar to bacterial urea transporters and reminiscent of their ancestral origins. Rapid equilibration of urea across the mitochondrial membrane may be vital for cell osmoregulation (elasmobranch) or nitrogen waste excretion (teleost).
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Zhong, Chongliang, Laura L. Griffin, Orla Heussaff, Ruairi O’Dea, Conor Whelan, and Gavin Stewart. "Sex-Related Differences in UT-B Urea Transporter Abundance in Fallow Deer Rumen." Veterinary Sciences 9, no. 2 (February 8, 2022): 73. http://dx.doi.org/10.3390/vetsci9020073.
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Rumen studies have focused almost exclusively on livestock species under strictly regimented diets. This means that the ruminal condition of free-living and free-feeding wildlife remains practically unstudied. Urea nitrogen salvaging, a process by which urea is passed into the rumen, to both provide a valuable source of nitrogen for bacterial growth and to buffer the potentially harmful acidic effects of bacterial short chain fatty acids, has remained unexplored in wild ruminants, such as deer. UT-B2 transporters are the key proteins reported to facilitate the transepithelial ruminal urea transport. In this study, we investigate the expression, abundance and localisation of urea transporters in the rumen of a semi-wild fallow deer (Dama dama) population. Physical measurements confirmed that males had larger rumen than females, while adults had longer papillae than juveniles. Initial RT-PCR experiments confirmed the expression of UT-B2, while immunolocalisation studies revealed that strong UT-B staining was present in the stratum basale of deer rumen. Western blotting analysis demonstrated that a 50 kDa UT-B2 protein was significantly more abundant in adult females compared to adult males. This study confirms the presence of UT-B2 urea transporters in deer rumen and suggests that sex-related differences occur, bringing new insight into our understanding of rumen physiology.
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Skouloubris, Stéphane, Jean-Michel Thiberge, Agnès Labigne, and Hilde De Reuse. "The Helicobacter pylori UreI Protein Is Not Involved in Urease Activity but Is Essential for Bacterial Survival In Vivo." Infection and Immunity 66, no. 9 (September 1, 1998): 4517–21. http://dx.doi.org/10.1128/iai.66.9.4517-4521.1998.
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ABSTRACT We produced defined isogenic Helicobacter pylori ureImutants to investigate the function of UreI, the product of one of the genes of the urease cluster. The insertion of a catcassette had a strong polar effect on the expression of the downstream urease genes, resulting in very weak urease activity. Urease activity, measured in vitro, was normal in a strain in which ureI was almost completely deleted and replaced with a nonpolar cassette. In contrast to previous reports, we thus found that the product ofureI was not necessary for the synthesis of active urease. Experiments with the mouse-adapted H. pylori SS1 strain carrying the nonpolar ureI deletion showed that UreI is essential for H. pylori survival in vivo and/or colonization of the mouse stomach. The replacement of ureIwith the nonpolar cassette strongly reduced H. pylorisurvival in acidic conditions (1-h incubation in phosphate-buffered saline solution at pH 2.2) in the presence of 10 mM urea. UreI is predicted to be an integral membrane protein and may therefore be involved in a transport process essential for H. pylori survival in vivo.
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Zeuthen, Thomas, Edurne Gorraitz, Ka Her, Ernest M. Wright, and Donald D. F. Loo. "Structural and functional significance of water permeation through cotransporters." Proceedings of the National Academy of Sciences 113, no. 44 (October 18, 2016): E6887—E6894. http://dx.doi.org/10.1073/pnas.1613744113.
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Membrane transporters, in addition to their major role as specific carriers for ions and small molecules, can also behave as water channels. However, neither the location of the water pathway in the protein nor their functional importance is known. Here, we map the pathway for water and urea through the intestinal sodium/glucose cotransporter SGLT1. Molecular dynamics simulations using the atomic structure of the bacterial transporter vSGLT suggest that water permeates the same path as Na+ and sugar. On a structural model of SGLT1, based on the homology structure of vSGLT, we identified and mutated residues lining the sugar transport pathway to cysteine. The mutants were expressed in Xenopus oocytes, and the unitary water and urea permeabilities were determined before and after modifying the cysteine side chain with reversible methanethiosulfonate reagents. The results demonstrate that water and urea follow the sugar transport pathway through SGLT1. The changes in permeability, increases or decreases, with side-chain modifications depend on the location of the mutation in the region of external or internal gates, or the sugar binding site. These changes in permeability are hypothesized to be due to alterations in steric hindrance to water and urea, and/or changes in protein folding caused by mismatching of side chains in the water pathway. Water permeation through SGLT1 and other transporters bears directly on the structural mechanism for the transport of polar solutes through these proteins. Finally, in vitro experiments on mouse small intestine show that SGLT1 accounts for two-thirds of the passive water flow across the gut.
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Wang, Jianxiu, Yanxia Long, Yu Zhao, Weiqiang Pan, Jianxun Qu, Tianliang Yang, Xinlei Huang, Xiaotian Liu, and Na Xu. "Laboratory Experiment on Formation of MICP Horizontal Seepage-Reducing Body in Confined Aquifer for Deep Excavation." Applied Sciences 13, no. 1 (December 22, 2022): 104. http://dx.doi.org/10.3390/app13010104.
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Using a soil improvement biotechnology based on microbial-induced carbonate precipitation (MICP) to form a horizontal water barrier in foundation pit dewatering can not only achieve a good dewatering control effect, but also control the cost and obtain good economic and environmental benefits. In this study, taking the Shanghai layer ⑨ sand as the research object, the solution injected into the layer ⑨ sand by MICP grouting technology includes bacterial solution (Sporosarcina pasteurii) and cementation solution (urea and CaCl2 solution). The migration mechanism of the bacterial solution and cementation solution in groundwater was analyzed through batch experiment and column test, and the mathematical model of migration was established. The dynamic adsorption characteristics of the S. pasteurii, Ca2+, and urea were obtained by dynamic adsorption test. Through isothermal adsorption test, the Freundlich isotherm was used to describe the isothermal adsorption of S. pasteurii onto fine sand, and the partition coefficient of the S. pasteurii was found to be 1.5 × 10−7 L/mg. The Langmuir isotherm can be used truly reflect the isothermal adsorption of Ca2+ onto fine sand. The distribution coefficient of the Ca2+ was 7 × 10−8 L/mg. The maximum adsorption capacity of the solute was 2404.8 mg/kg. The adsorption capacity of the urea was very small. According to the sand column test, the vertical dispersion was 11.5 cm. Due to the obvious size effect of dispersion, the sensitivity of dispersion in actual working conditions should be analyzed in a subsequent numerical simulation. The determined solute transport parameters provide support for the further study of the numerical simulation of the solute transport process of the HSRB formed by MICP grouting technology and provide a basis for further field application.
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Sanders, M. R., H. E. Findlay, and P. J. Booth. "Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein." Proceedings of the National Academy of Sciences 115, no. 8 (February 5, 2018): E1799—E1808. http://dx.doi.org/10.1073/pnas.1714668115.
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α-Helical membrane proteins have eluded investigation of their thermodynamic stability in lipid bilayers. Reversible denaturation curves have enabled some headway in determining unfolding free energies. However, these parameters have been limited to detergent micelles or lipid bicelles, which do not possess the same mechanical properties as lipid bilayers that comprise the basis of natural membranes. We establish reversible unfolding of the membrane transporter LeuT in lipid bilayers, enabling the comparison of apparent unfolding free energies in different lipid compositions. LeuT is a bacterial ortholog of neurotransmitter transporters and contains a knot within its 12-transmembrane helical structure. Urea is used as a denaturant for LeuT in proteoliposomes, resulting in the loss of up to 30% helical structure depending upon the lipid bilayer composition. Urea unfolding of LeuT in liposomes is reversible, with refolding in the bilayer recovering the original helical structure and transport activity. A linear dependence of the unfolding free energy on urea concentration enables the free energy to be extrapolated to zero denaturant. Increasing lipid headgroup charge or chain lateral pressure increases the thermodynamic stability of LeuT. The mechanical and charge properties of the bilayer also affect the ability of urea to denature the protein. Thus, we not only gain insight to the long–sought-after thermodynamic stability of an α-helical protein in a lipid bilayer but also provide a basis for studies of the folding of knotted proteins in a membrane environment.
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Moran, M. A., R. Belas, M. A. Schell, J. M. González, F. Sun, S. Sun, B. J. Binder, et al. "Ecological Genomics of Marine Roseobacters." Applied and Environmental Microbiology 73, no. 14 (May 25, 2007): 4559–69. http://dx.doi.org/10.1128/aem.02580-06.
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ABSTRACT Bacterioplankton of the marine Roseobacter clade have genomes that reflect a dynamic environment and diverse interactions with marine plankton. Comparative genome sequence analysis of three cultured representatives suggests that cellular requirements for nitrogen are largely provided by regenerated ammonium and organic compounds (polyamines, allophanate, and urea), while typical sources of carbon include amino acids, glyoxylate, and aromatic metabolites. An unexpectedly large number of genes are predicted to encode proteins involved in the production, degradation, and efflux of toxins and metabolites. A mechanism likely involved in cell-to-cell DNA or protein transfer was also discovered: vir-related genes encoding a type IV secretion system typical of bacterial pathogens. These suggest a potential for interacting with neighboring cells and impacting the routing of organic matter into the microbial loop. Genes shared among the three roseobacters and also common in nine draft Roseobacter genomes include those for carbon monoxide oxidation, dimethylsulfoniopropionate demethylation, and aromatic compound degradation. Genes shared with other cultured marine bacteria include those for utilizing sodium gradients, transport and metabolism of sulfate, and osmoregulation.