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Journal articles on the topic 'Proteoliposome transporter'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Cosco, Jessica, Teresa M. R. Regina, Mariafrancesca Scalise, Michele Galluccio, and Cesare Indiveri. "Regulatory Aspects of the Vacuolar CAT2 Arginine Transporter of S. lycopersicum: Role of Osmotic Pressure and Cations." International Journal of Molecular Sciences 20, no. 4 (2019): 906. http://dx.doi.org/10.3390/ijms20040906.

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Many proteins are localized at the vacuolar membrane, but most of them are still poorly described, due to the inaccessibility of this membrane from the extracellular environment. This work focused on the characterization of the CAT2 transporter from S. lycopersicum (SlCAT2) that was previously overexpressed in E. coli and reconstituted in proteoliposomes for transport assay as [3H]Arg uptake. The orientation of the reconstituted transporter has been attempted and current data support the hypothesis that the protein is inserted in the liposome in the same orientation as in the vacuole. SlCAT2 a

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2

Pochini, Lorena, Gilda Pappacoda, Michele Galluccio, Francesco Pastore, Mariafrancesca Scalise, and Cesare Indiveri. "Effect of Cholesterol on the Organic Cation Transporter OCTN1 (SLC22A4)." International Journal of Molecular Sciences 21, no. 3 (2020): 1091. http://dx.doi.org/10.3390/ijms21031091.

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The effect of cholesterol was investigated on the OCTN1 transport activity measured as [14C]-tetraethylamonium or [3H]-acetylcholine uptake in proteoliposomes reconstituted with native transporter extracted from HeLa cells or the human recombinant OCTN1 over-expressed in E. coli. Removal of cholesterol from the native transporter by MβCD before reconstitution led to impairment of transport activity. A similar activity impairment was observed after treatment of proteoliposomes harboring the recombinant (cholesterol-free) protein by MβCD, suggesting that the lipid mixture used for reconstitution

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3

Hakim Elahi, Sepideh, Morteza Abbaszadegan, and Otakuye Conroy-Ben. "Engineered proteoliposome transporter for treatment of cesium contaminated water." Science of The Total Environment 704 (February 2020): 135317. http://dx.doi.org/10.1016/j.scitotenv.2019.135317.

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4

Wan, Hao, Chengfeng Merriman, Mark A. Atkinson, et al. "Proteoliposome-based full-length ZnT8 self-antigen for type 1 diabetes diagnosis on a plasmonic platform." Proceedings of the National Academy of Sciences 114, no. 38 (2017): 10196–201. http://dx.doi.org/10.1073/pnas.1711169114.

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Identified as a major biomarker for type 1 diabetes (T1D) diagnosis, zinc transporter 8 autoantibody (ZnT8A) has shown promise for staging disease risk and disease diagnosis. However, existing assays for ZnT8 autoantibody (ZnT8A) are limited to detection by soluble domains of ZnT8, owing to difficulties in maintaining proper folding of a full-length ZnT8 protein outside its native membrane environment. Through a combined bioengineering and nanotechnology approach, we have developed a proteoliposome-based full-length ZnT8 self-antigen (full-length ZnT8 proteoliposomes; PLR-ZnT8) for efficient d

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5

Rajagopalan, Nandhakishore, Annamaria Halasz, Yuping Lu, Enwu Liu, Fanny Monteil-Rivera, and Michele C. Loewen. "Probing allocrite preferences of 2 naturally occurring variants of the wheat LR34 ABC transporter." Biochemistry and Cell Biology 94, no. 5 (2016): 459–70. http://dx.doi.org/10.1139/bcb-2016-0058.

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For almost a century, the wheat Lr34 gene has conferred durable resistance against fungal rust diseases. While sequence homology predicts a putative ATP binding cassette transporter, the molecules that are transported (allocrites) by the encoded LR34 variants, and any associated mechanism of resistance, remain enigmatic. Here, the in vitro transport characteristics of 2 naturally occurring Lr34 variants (that differ in their ability to mediate disease resistance; Lr34sus and Lr34res) are investigated. Initially, a method to express and purify recombinant LR34Sus and LR34Res pseudo half-molecul

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6

Togawa, Natsuko, Narinobu Juge, Takaaki Miyaji, Miki Hiasa, Hiroshi Omote, and Yoshinori Moriyama. "Wide expression of type I Na+-phosphate cotransporter 3 (NPT3/SLC17A2), a membrane potential-driven organic anion transporter." American Journal of Physiology-Cell Physiology 309, no. 2 (2015): C71—C80. http://dx.doi.org/10.1152/ajpcell.00048.2015.

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Membrane potential (Δψ)-driven and Cl−-dependent organic anion transport is a primary function of the solute carrier family 17 (SLC17) transporter family. Although the transport substrates and physiological relevance of the major members are well understood, SLC17A2 protein known to be Na+-phosphate cotransporter 3 (NPT3) is far less well characterized. In the present study, we investigated the transport properties and expression patterns of mouse SLC17A2 protein (mNPT3). Proteoliposomes containing the purified mNPT3 protein took up radiolabeled p-aminohippuric acid (PAH) in a Δψ- and Cl−-depe

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7

Rautengarten, Carsten, Devon Birdseye, Sivakumar Pattathil, et al. "The elaborate route for UDP-arabinose delivery into the Golgi of plants." Proceedings of the National Academy of Sciences 114, no. 16 (2017): 4261–66. http://dx.doi.org/10.1073/pnas.1701894114.

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In plants, L-arabinose (Ara) is a key component of cell wall polymers, glycoproteins, as well as flavonoids, and signaling peptides. Whereas the majority of Ara found in plant glycans occurs as a furanose ring (Araf), the activated precursor has a pyranose ring configuration (UDP-Arap). The biosynthesis of UDP-Arap mainly occurs via the epimerization of UDP-xylose (UDP-Xyl) in the Golgi lumen. Given that the predominant Ara form found in plants is Araf, UDP-Arap must exit the Golgi to be interconverted into UDP-Araf by UDP-Ara mutases that are located outside on the cytosolic surface of the Go

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8

Chin, J. J., E. K. Jung, V. Chen, and C. Y. Jung. "Structural basis of human erythrocyte glucose transporter function in proteoliposome vesicles: circular dichroism measurements." Proceedings of the National Academy of Sciences 84, no. 12 (1987): 4113–16. http://dx.doi.org/10.1073/pnas.84.12.4113.

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9

Boadu, Emmanuel, and Georg Sager. "ATPase activity and transport by a cGMP transporter in human erythrocyte ghosts and proteoliposome-reconstituted membrane extracts." Biochimica et Biophysica Acta (BBA) - Biomembranes 1509, no. 1-2 (2000): 467–74. http://dx.doi.org/10.1016/s0005-2736(00)00328-x.

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10

Tonazzi, Annamaria, Ivano Eberini, and Cesare Indiveri. "Molecular Mechanism of Inhibition of the Mitochondrial Carnitine/Acylcarnitine Transporter by Omeprazole Revealed by Proteoliposome Assay, Mutagenesis and Bioinformatics." PLoS ONE 8, no. 12 (2013): e82286. http://dx.doi.org/10.1371/journal.pone.0082286.

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11

Pochini, Lorena, Valentina Peta, and Cesare Indiveri. "Inhibition of the OCTN2 carnitine transporter by HgCl2and methylmercury in the proteoliposome experimental model: insights in the mechanism of toxicity." Toxicology Mechanisms and Methods 23, no. 2 (2012): 68–76. http://dx.doi.org/10.3109/15376516.2012.719166.

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12

Pochini, Lorena, Angela Seidita, Cristina Sensi, Mariafrancesca Scalise, Ivano Eberini, and Cesare Indiveri. "Nimesulide binding site in the B0AT1 (SLC6A19) amino acid transporter. Mechanism of inhibition revealed by proteoliposome transport assay and molecular modelling." Biochemical Pharmacology 89, no. 3 (2014): 422–30. http://dx.doi.org/10.1016/j.bcp.2014.03.014.

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13

Brekkan, Eggert, Andreas Lundqvist, and Per Lundahl. "Immobilized Membrane Vesicle or Proteoliposome Affinity Chromatography. Frontal Analysis of Interactions of Cytochalasin B andd-Glucose with the Human Red Cell Glucose Transporter†." Biochemistry 35, no. 37 (1996): 12141–45. http://dx.doi.org/10.1021/bi9603231.

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14

MÖHLMANN, Torsten, Joachim TJADEN, Gundrun HENRICHS, Paul W. QUICK, Rainer HÄUSLER, and Ekkehard H. NEUHAUS. "ADP-glucose drives starch synthesis in isolated maize endosperm amyloplasts: characterization of starch synthesis and transport properties across the amyloplast envelope." Biochemical Journal 324, no. 2 (1997): 503–9. http://dx.doi.org/10.1042/bj3240503.

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We recently developed a method of purifying amyloplasts from developing maize (Zea mays L.) endosperm tissue [Neuhaus, Thom, Batz and Scheibe (1993) Biochem. J. 296, 395–401]. In the present paper we analyse how glucose 6-phosphate (Glc6P) and other phosphorylated compounds enter the plastid compartment. Using a proteoliposome system in which the plastid envelope membrane proteins are functionally reconstituted, we demonstrate that this type of plastid is able to transport [14C]Glc6P or [32P]Pi in counter exchange with Pi, Glc6P, dihydroxyacetone phosphate and phosphoenolpyruvate. Glucose 1-ph

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15

Yu, Haijia, Shailendra S. Rathore, Eric M. Davis, Yan Ouyang, and Jingshi Shen. "Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending–dependent manner." Molecular Biology of the Cell 24, no. 8 (2013): 1176–84. http://dx.doi.org/10.1091/mbc.e12-11-0810.

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The glucose transporter GLUT4 plays a central role in maintaining body glucose homeostasis. On insulin stimulation, GLUT4-containing vesicles fuse with the plasma membrane, relocating GLUT4 from intracellular reservoirs to the cell surface to uptake excess blood glucose. The GLUT4 vesicle fusion reaction requires soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) as the core fusion engine and a group of regulatory proteins. In particular, the soluble C2-domain factor Doc2b plays a key role in GLUT4 vesicle fusion, but its molecular mechanism has been unclear. Here

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16

Visser, Wouter F., Carlo W. van Roermund, Lodewijk Ijlst, Klaas J. Hellingwerf, Ronald J. A. Wanders, and Hans R. Waterham. "Demonstration and characterization of phosphate transport in mammalian peroxisomes." Biochemical Journal 389, no. 3 (2005): 717–22. http://dx.doi.org/10.1042/bj20041846.

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It is now well established that the peroxisomal membrane is not freely permeable to small molecules in vivo, which implies the existence of metabolite transporters in the peroxisomal membrane. A few putative peroxisomal metabolite transporters have indeed been identified, but the function of these proteins has remained largely unresolved so far. The only peroxisomal transporter characterized to a significant extent is the adenine nucleotide transporter, which is presumably required to sustain the activity of the intraperoxisomal very-long-chain-acyl-CoA synthetase. In addition to AMP, this acy

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17

Console, Lara, Maria Tolomeo, Matilde Colella, Maria Barile, and Cesare Indiveri. "Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli." International Journal of Molecular Sciences 20, no. 18 (2019): 4416. http://dx.doi.org/10.3390/ijms20184416.

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Background: the SLC52A2 gene encodes for the riboflavin transporter 2 (RFVT2). This transporter is ubiquitously expressed. It mediates the transport of Riboflavin across cell membranes. Riboflavin plays a crucial role in cells since its biologically active forms, FMN and FAD, are essential for the metabolism of carbohydrates, amino acids, and lipids. Mutation of the Riboflavin transporters is a risk factor for anemia, cancer, cardiovascular disease, neurodegeneration. Inborn mutations of SLC52A2 are associated with Brown-Vialetto-van Laere syndrome, a rare neurological disorder characterized b

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18

Yang, Qing, and Per Lundahl. "Immobilized Proteoliposome Affinity Chromatography for Quantitative Analysis of Specific Interactions between Solutes and Membrane Proteins. Interaction of Cytochalasin B andd-Glucose with the Glucose Transporter Glut1." Biochemistry 35, no. 33 (1996): 11012. http://dx.doi.org/10.1021/bi965011c.

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19

Yang, Qing, and Per Lundahl. "Immobilized Proteoliposome Affinity Chromatography for Quantitative Analysis of Specific Interactions between Solutes and Membrane Proteins. Interaction of Cytochalasin B and D-Glucose with the Glucose Transporter Glut1." Biochemistry 34, no. 22 (1995): 7289–94. http://dx.doi.org/10.1021/bi00022a001.

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20

Pochini, Lorena, Mariafrancesca Scalise, Michele Galluccio, and Cesare Indiveri. "OCTN Cation Transporters in Health and Disease." Journal of Biomolecular Screening 18, no. 8 (2013): 851–67. http://dx.doi.org/10.1177/1087057113493006.

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The three members of the organic cation transporter novel subfamily are known to be involved in interactions with xenobiotic compounds. These proteins are characterized by 12 transmembrane segments connected by nine short loops and two large hydrophilic loops. It has been recently pointed out that acetylcholine is a physiological substrate of OCTN1. Its transport could be involved in nonneuronal cholinergic functions. OCTN2 maintains the carnitine homeostasis, resulting from intestinal absorption, distribution to tissues, and renal excretion/reabsorption. OCTN3, identified only in mouse, media

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21

Zharikov, S. I., and E. R. Block. "Association of l-arginine transporters with fodrin: implications for hypoxic inhibition of arginine uptake." American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (2000): L111—L117. http://dx.doi.org/10.1152/ajplung.2000.278.1.l111.

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In this study, we investigated the possible interaction between the cationic amino acid transporter (CAT)-1 arginine transporter and ankyrin or fodrin. Because ankyrin and fodrin are substrates for calpain and because hypoxia increases calpain expression and activity in pulmonary artery endothelial cells (PAEC), we also studied the effect of hypoxia on ankyrin, fodrin, and CAT-1 contents in PAEC. Exposure to long-term hypoxia (24 h) inhibited l-arginine uptake by PAEC, and this inhibition was prevented by calpain inhibitor 1. The effects of hypoxia and calpain inhibitor 1 were not associated w

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22

Ramamoorthy, S., D. R. Cool, F. H. Leibach, V. B. Mahesh, and V. Ganapathy. "Reconstitution of the human placental 5-hydroxytryptamine transporter in a catalytically active form after detergent solubilization." Biochemical Journal 286, no. 1 (1992): 89–95. http://dx.doi.org/10.1042/bj2860089.

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The 5-hydroxytryptamine (5-HT; serotonin) transporter was solubilized from purified human placental brush border membranes by cholate in the presence of urea, and the solubilized transporter was reconstituted into proteoliposomes in a functionally active form. Solubilization of the membranes with cholate in the absence of urea inactivated the transporter. The reconstitution procedure involved precipitation of the solubilized proteins and simultaneous removal of cholate and urea by poly(ethylene glycol), and incorporation of the precipitated proteins into proteoliposomes in the presence of asol

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23

Hürlimann, Lea M., Valentina Corradi, Michael Hohl, Guido V. Bloemberg, D. Peter Tieleman, and Markus A. Seeger. "The Heterodimeric ABC Transporter EfrCD Mediates Multidrug Efflux in Enterococcus faecalis." Antimicrobial Agents and Chemotherapy 60, no. 9 (2016): 5400–5411. http://dx.doi.org/10.1128/aac.00661-16.

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ABSTRACTNosocomial infections withEnterococcus faecalisare an emerging health problem. However, drug efflux pumps contributing to intrinsic drug resistance are poorly studied in this Gram-positive pathogen. In this study, we functionally investigated seven heterodimeric ABC transporters ofE. faecalisthat are annotated as drug efflux pumps. Deletion ofef0789-ef0790on the chromosome ofE. faecalisresulted in increased susceptibility to daunorubicin, doxorubicin, ethidium, and Hoechst 33342, and the corresponding transporter was named EfrCD. Unexpectedly, the previously described heterodimeric mul

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24

Debiec, H., R. Lorenc, and P. M. Ronco. "Reconstitution and characterization of a Na+/Pi co-transporter protein from rabbit kidney brush-border membranes." Biochemical Journal 286, no. 1 (1992): 97–102. http://dx.doi.org/10.1042/bj2860097.

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A protein with Na+/Pi co-transporter activity has been extracted from rabbit brush-border membranes with chloroform/methanol and purified by hydroxyapatite chromatography. The protein has been incorporated by the dilution method into liposomes formed from different types and ratios of lipids. The greatest reconstitution has been achieved into liposomes prepared from cholesterol (20%), phosphatidylcholine (20%), phosphatidylethanolamine (30%) and phosphatidylserine (30%) (CH/PC/PE/PS). Pi uptake by these proteoliposomes had the following characteristics: (i) the initial rate was markedly greate

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Yu, Jian-Lin, Leo Grinius, and David C. Hooper. "NorA Functions as a Multidrug Efflux Protein in both Cytoplasmic Membrane Vesicles and Reconstituted Proteoliposomes." Journal of Bacteriology 184, no. 5 (2002): 1370–77. http://dx.doi.org/10.1128/jb.184.5.1370-1377.2002.

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ABSTRACT Overexpression of NorA, an endogenous efflux transporter of Staphylococcus aureus, confers resistance to certain fluoroquinolone antimicrobials and diverse other substrates. The norA gene was amplified by PCR and cloned in the expression vector pTrcHis2. Histidine-tagged NorA (NorA-His) was overexpressed in Escherichia coli cells to prepare two experimental systems, everted membrane vesicles enriched with NorA-His and proteoliposomes reconstituted with purified NorA-His. In membrane vesicles, NorA-His actively transported Hoechst 33342, a dye that is strongly fluorescent in the membra

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Zollmann, Tina, Gemma Moiset, Franz Tumulka, Robert Tampé, Bert Poolman, and Rupert Abele. "Single liposome analysis of peptide translocation by the ABC transporter TAPL." Proceedings of the National Academy of Sciences 112, no. 7 (2015): 2046–51. http://dx.doi.org/10.1073/pnas.1418100112.

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ATP-binding cassette (ABC) transporters use ATP to drive solute transport across biological membranes. Members of this superfamily have crucial roles in cell physiology, and some of the transporters are linked to severe diseases. However, understanding of the transport mechanism, especially of human ABC exporters, is scarce. We reconstituted the human lysosomal polypeptide ABC transporter TAPL, expressed inPichia pastoris, into lipid vesicles (liposomes) and performed explicit transport measurements. We analyzed solute transport at the single liposome level by monitoring the coincident fluores

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27

Lodder-Gadaczek, Julia, Volkmar Gieselmann, and Matthias Eckhardt. "Vesicular uptake of N-acetylaspartylglutamate is catalysed by sialin (SLC17A5)." Biochemical Journal 454, no. 1 (2013): 31–38. http://dx.doi.org/10.1042/bj20130300.

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NAAG (N-acetylaspartylglutamate) is an abundant neuropeptide in the vertebrate nervous system. It is released from synaptic terminals in a calcium-dependent manner and has been shown to act as an agonist at the type II metabotropic glutamate receptor mGluR3. It has been proposed that NAAG may also be released from axons. So far, however, it has remained unclear how NAAG is transported into synaptic or other vesicles before it is secreted. In the present study, we demonstrate that uptake of NAAG and the related peptide NAAG2 (N-acetylaspartylglutamylglutamate) into vesicles depends on the siali

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28

Kaler, P., and R. Prasad. "Molecular cloning and functional characterization of novel zinc transporter rZip10 (Slc39a10) involved in zinc uptake across rat renal brush-border membrane." American Journal of Physiology-Renal Physiology 292, no. 1 (2007): F217—F229. http://dx.doi.org/10.1152/ajprenal.00014.2006.

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Previously, in our laboratory a 40-kDa zinc transporter protein was purified and functionally reconstituted in proteoliposomes (Kumar R, Prasad R. Biochim Biophys Acta 1419: 23–32, 1999). Furthermore, we now report the identification of Slc39a10 cDNA encoding the 40-kDa zinc transporter protein by isolating a cloned DNA complementary to zinc transporter mRNA. cDNA was constructed from immunoenriched mRNA encoding the zinc transporter. cDNA was inserted into pBR322 using poly(dC)- poly(dG) tailing. Escherichia coli DH5α cells were transformed, and colonies were screened for zinc transporter cDN

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29

Sakamoto, Kanta, Abelardo Margolles, Hendrik W. van Veen, and Wil N. Konings. "Hop Resistance in the Beer Spoilage Bacterium Lactobacillus brevis Is Mediated by the ATP-Binding Cassette Multidrug Transporter HorA." Journal of Bacteriology 183, no. 18 (2001): 5371–75. http://dx.doi.org/10.1128/jb.183.18.5371-5375.2001.

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ABSTRACT Lactobacillus brevis is a major contaminant of spoiled beer. The organism can grow in beer in spite of the presence of antibacterial hop compounds that give the beer a bitter taste. The hop resistance in L. brevis is, at least in part, dependent on the expression of the horA gene. The deduced amino acid sequence of HorA is 53% identical to that of LmrA, an ATP-binding cassette multidrug transporter in Lactococcus lactis. To study the role of HorA in hop resistance, HorA was functionally expressed in L. lactis as a hexa-histidine-tagged protein using the nisin-controlled gene expressio

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30

Hall, Jason A., and Ana M. Pajor. "Functional Reconstitution of SdcS, a Na+-Coupled Dicarboxylate Carrier Protein from Staphylococcus aureus." Journal of Bacteriology 189, no. 3 (2006): 880–85. http://dx.doi.org/10.1128/jb.01452-06.

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ABSTRACT In Staphylococcus aureus, the transport of dicarboxylates is mediated in part by the Na+-linked carrier protein SdcS. This transporter is a member of the divalent-anion/Na+ symporter (DASS) family, a group that includes the mammalian Na+/dicarboxylate cotransporters NaDC1 and NaDC3. In earlier work, we cloned and expressed SdcS in Escherichia coli and found it to have transport properties similar to those of its eukaryotic counterparts (J. A. Hall and A. M. Pajor, J. Bacteriol. 187:5189-5194, 2005). Here, we report the partial purification and subsequent reconstitution of functional S

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31

Reich-Slotky, Ronit, Cynthia Panagiotidis, Moraima Reyes, and Howard A. Shuman. "The Detergent-Soluble Maltose Transporter Is Activated by Maltose Binding Protein and Verapamil." Journal of Bacteriology 182, no. 4 (2000): 993–1000. http://dx.doi.org/10.1128/jb.182.4.993-1000.2000.

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ABSTRACT The maltose transporter FGK2 complex of Escherichia coli was purified with the aid of a glutathioneS-transferase molecular tag. In contrast to the membrane-associated form of the complex, which requires liganded maltose binding protein (MBP) for ATPase activity, the purified detergent-soluble complex exhibited a very high level of ATPase activity. This uncoupled activity was not due to dissociation of the MalK ATPase subunit from the integral membrane protein MalF and MalG subunits. The detergent-soluble ATPase activity of the complex could be further stimulated by wild-type MBP but n

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Pordy, W. T., M. S. Lipkowitz, and R. G. Abramson. "Evidence for the transport function of uricase, an oxidative enzyme." American Journal of Physiology-Renal Physiology 253, no. 4 (1987): F702—F711. http://dx.doi.org/10.1152/ajprenal.1987.253.4.f702.

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[2-14C]urate uptake was examined in proteoliposomes prepared with phosphatidylcholine and either pig liver uricase or albumin, and in protein-free liposomes. Urate uptake was only evident in proteoliposomes that contained active uricase. Uptakes were indistinguishable in the presence and absence of inwardly directed gradients of sodium, potassium, or choline chloride or outwardly directed hydroxyl gradients. Both urate and allantoin accumulated within proteoliposomes during urate uptake; however, [2–14C]allantoin was not taken up by proteoliposomes. Urate uptake was accelerated in the presence

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Aires, Julio Ramos, and Hiroshi Nikaido. "Aminoglycosides Are Captured from both Periplasm and Cytoplasm by the AcrD Multidrug Efflux Transporter of Escherichia coli." Journal of Bacteriology 187, no. 6 (2005): 1923–29. http://dx.doi.org/10.1128/jb.187.6.1923-1929.2005.

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ABSTRACT To understand better the mechanisms of resistance-nodulation-division (RND)-type multidrug efflux pumps, we examined the Escherichia coli AcrD pump, whose typical substrates, aminoglycosides, are not expected to diffuse spontaneously across the lipid bilayer. The hexahistidine-tagged AcrD protein was purified and reconstituted into unilamellar proteoliposomes. Its activity was measured by the proton flux accompanying substrate transport. When the interior of the proteoliposomes was acidified, the addition of aminoglycosides to the external medium stimulated proton efflux and the intra

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TETLOW, Ian J., Caroline G. BOWSHER, and Michael J. EMES. "Reconstitution of the hexose phosphate translocator from the envelope membranes of wheat endosperm amyloplasts." Biochemical Journal 319, no. 3 (1996): 717–23. http://dx.doi.org/10.1042/bj3190717.

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Amyloplasts were isolated and purified from wheat endosperm and the envelope membranes reconstituted into liposomes. Envelope membranes were solubilized in n-octyl β-D-glucopyranoside and mixed with liposomes supplemented with 5.6 mol% cholesterol to produce proteoliposomes of defined size, which showed negligible leakage of internal substrates. Transport experiments with proteoliposomes revealed a counter-exchange of glucose 1-phosphate (Glc1P), glucose 6-phosphate (Glc6P), inorganic phosphate (Pi), 3-phosphoglycerate and dihydroxyacetone phosphate. The Glc1P/Pi counter-exchange reaction exhi

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35

Sharma, Susan, Johnny A. Davis, Tulin Ayvaz, Beth Traxler, and Amy L. Davidson. "Functional Reassembly of the Escherichia coli Maltose Transporter following Purification of a MalF-MalG Subassembly." Journal of Bacteriology 187, no. 8 (2005): 2908–11. http://dx.doi.org/10.1128/jb.187.8.2908-2911.2005.

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ABSTRACT Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK2 maltose transporter complex both in detergent solution and in proteoliposomes.

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PARKER, JOHN R., and KENNETH P. WHEELER. "Proteins present in proteoliposomes containing an Na+-dependent alanine transporter." Biochemical Society Transactions 16, no. 3 (1988): 344–45. http://dx.doi.org/10.1042/bst0160344.

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37

SHAROM, Frances J., Xiaohong YU, Giulio DiDIODATO, and Joseph W. K. CHU. "Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport." Biochemical Journal 320, no. 2 (1996): 421–28. http://dx.doi.org/10.1042/bj3200421.

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P-Glycoprotein functions as an ATP-driven active efflux pump for many natural products and chemotherapeutic drugs. Hydrophobic peptides have been shown to block drug uptake by P-glycoprotein, indicating that they might be transport substrates. The present study examines the interaction of the synthetic peptide series NAc-LnY-amide with the multidrug transporter. Several peptides in this series caused up to 3.5-fold enhancement of colchicine accumulation in membrane vesicles from multidrug resistant (MDR) cells, which suggests the existence of novel interactions between the binding sites for pe

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Welch, Alexander, Chidiebere U. Awah, Shiheng Jing, Hendrik W. van Veen, and Henrietta Venter. "Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa." Biochemical Journal 430, no. 2 (2010): 355–64. http://dx.doi.org/10.1042/bj20091860.

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The MexAB–OprM drug efflux pump is central to multidrug resistance of Pseudomonas aeruginosa. The ability of the tripartite protein to confer drug resistance on the pathogen is crucially dependent on the presence of all three proteins of the complex. However, the role of each protein in the formation of the intact functional complex is not well understood. One of the key questions relates to the (in)ability of MexB to act independently of its cognitive partners, MexA and OprM. In the present study, we have demonstrated that, in the absence of MexA and OprM, MexB can: (i) recruit AcrA and TolC

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Vachon, V., M. C. Delisle, R. Laprade, and R. Béliveau. "Reconstitution of the renal brush-border membrane sodium/phosphate co-transporter." Biochemical Journal 278, no. 2 (1991): 543–48. http://dx.doi.org/10.1042/bj2780543.

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A simple and rapid procedure was developed for the reconstitution of Na(+)-dependent phosphate-transport activity from bovine kidney brush-border membranes. The phosphate transporter appears to be particularly sensitive to extraction conditions. To prevent its inactivation, the phosphate carrier was solubilized in a buffer containing its substrates, Na+ and phosphate, CHAPS, dithiothreitol, brush-border membrane lipids and glycerol. The uptake of phosphate by reconstituted vesicles was strongly stimulated by the presence of a transmembrane Na+ gradient. This stimulation was abolished when the

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Amati, Andrea Marco, Simone Graf, Sabina Deutschmann, Nicolas Dolder, and Christoph von Ballmoos. "Current problems and future avenues in proteoliposome research." Biochemical Society Transactions 48, no. 4 (2020): 1473–92. http://dx.doi.org/10.1042/bst20190966.

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Membrane proteins (MPs) are the gatekeepers between different biological compartments separated by lipid bilayers. Being receptors, channels, transporters, or primary pumps, they fulfill a wide variety of cellular functions and their importance is reflected in the increasing number of drugs that target MPs. Functional studies of MPs within a native cellular context, however, is difficult due to the innate complexity of the densely packed membranes. Over the past decades, detergent-based extraction and purification of MPs and their reconstitution into lipid mimetic systems has been a very power

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Matsuo, Shunsuke, Miki Hiasa, and Hiroshi Omote. "Functional characterization and tissue localization of the facilitative glucose transporter GLUT12." Journal of Biochemistry 168, no. 6 (2020): 611–20. http://dx.doi.org/10.1093/jb/mvaa090.

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Abstract Facilitative glucose transporters (GLUTs) play crucial roles in glucose utilization and homeostasis. GLUT12 was initially isolated as a novel GLUT4-like transporter involved in insulin-dependent glucose transport. However, tissue distribution and biochemical properties of GLUT12 are not well understood. In this study, we investigated the basic kinetic properties and tissue distribution of GLUT12. Human GLUT12 and GLUT1 were overexpressed and purified using Ni-NTA column chromatography. Reconstituted proteoliposomes showed time-dependent d-glucose transport activity, which was inhibite

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Nagamori, Shushi, Pattama Wiriyasermkul, Meritxell Espino Guarch, et al. "Novel cystine transporter in renal proximal tubule identified as a missing partner of cystinuria-related plasma membrane protein rBAT/SLC3A1." Proceedings of the National Academy of Sciences 113, no. 3 (2016): 775–80. http://dx.doi.org/10.1073/pnas.1519959113.

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Heterodimeric amino acid transporters play crucial roles in epithelial transport, as well as in cellular nutrition. Among them, the heterodimer of a membrane protein b0,+AT/SLC7A9 and its auxiliary subunit rBAT/SLC3A1 is responsible for cystine reabsorption in renal proximal tubules. The mutations in either subunit cause cystinuria, an inherited amino aciduria with impaired renal reabsorption of cystine and dibasic amino acids. However, an unsolved paradox is that rBAT is highly expressed in the S3 segment, the late proximal tubules, whereas b0,+AT expression is highest in the S1 segment, the

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Shin, Seung Jin, Woo Kyoung Lee, Hyung Wook Lim, and Jong-Sang Park. "Characterization of the ATP transporter in the reconstituted rough endoplasmic reticulum proteoliposomes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1468, no. 1-2 (2000): 55–62. http://dx.doi.org/10.1016/s0005-2736(00)00241-8.

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Scalise, Mariafrancesca, Lorena Pochini, Nicola Giangregorio, Annamaria Tonazzi, and Cesare Indiveri. "Proteoliposomes as Tool for Assaying Membrane Transporter Functions and Interactions with Xenobiotics." Pharmaceutics 5, no. 4 (2013): 472–97. http://dx.doi.org/10.3390/pharmaceutics5030472.

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Seelheim, Patrick, Michael Seifert, and Hans-Joachim Galla. "New Immobilized Proteoliposome-Based Biosensor System for Investigating Human ATP-Binding Cassette Transporters." Biophysical Journal 98, no. 3 (2010): 684a—685a. http://dx.doi.org/10.1016/j.bpj.2009.12.3760.

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Sharma, Rajendra, Abha Sharma, Yusong Yang, et al. "Functional reconstitution of Ral-binding GTPase activating protein, RLIP76, in proteoliposomes catalyzing ATP-dependent transport of glutathione conjugate of 4-hydroxynonenal." Acta Biochimica Polonica 49, no. 3 (2002): 693–701. http://dx.doi.org/10.18388/abp.2002_3778.

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Earlier studies from our laboratories have shown that RLIP76, a previously described Ral-binding GTPase activating protein (Jullien-Flores et al., 1995, J. Biol. Chem. 270: 22473), is identical with the xenobiotic transporter DNP-SG ATPase, and can catalyze ATP-dependent transport of glutathione-conjugates as well as doxorubin (Awasthi et al., 2000, Biochemistry, 39: 9327). We have now reconstituted purified bacterially expressed RLIP76 in proteoliposomes, and have studied ATP-dependent uptake of the glutathione conjugate of 4-hydroxynonenal (GS-HNE) by these vesicles. Results of these studies

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Ishijima, Sumio, Zenpei Shigemi, Hiroaki Adachi, Nana Makinouchi, and Ikuko Sagami. "Functional reconstitution and characterization of the Arabidopsis Mg2+ transporter AtMRS2-10 in proteoliposomes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1818, no. 9 (2012): 2202–8. http://dx.doi.org/10.1016/j.bbamem.2012.04.015.

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Wood, Janet M. "Osmosensing by Bacteria: Signals and Membrane-Based Sensors." Microbiology and Molecular Biology Reviews 63, no. 1 (1999): 230–62. http://dx.doi.org/10.1128/mmbr.63.1.230-262.1999.

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SUMMARY Bacteria can survive dramatic osmotic shifts. Osmoregulatory responses mitigate the passive adjustments in cell structure and the growth inhibition that may ensue. The levels of certain cytoplasmic solutes rise and fall in response to increases and decreases, respectively, in extracellular osmolality. Certain organic compounds are favored over ions as osmoregulatory solutes, although K+ fluxes are intrinsic to the osmoregulatory response for at least some organisms. Osmosensors must undergo transitions between “off” and “on” conformations in response to changes in extracellular water a

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Tempelhagen, Laura, Anita Ayer, Doreen E. Culham, Roland Stocker, and Janet M. Wood. "Cultivation at high osmotic pressure confers ubiquinone 8–independent protection of respiration on Escherichia coli." Journal of Biological Chemistry 295, no. 4 (2019): 981–93. http://dx.doi.org/10.1074/jbc.ra119.011549.

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Ubiquinone 8 (coenzyme Q8 or Q8) mediates electron transfer within the aerobic respiratory chain, mitigates oxidative stress, and contributes to gene expression in Escherichia coli. In addition, Q8 was proposed to confer bacterial osmotolerance by accumulating during growth at high osmotic pressure and altering membrane stability. The osmolyte trehalose and membrane lipid cardiolipin accumulate in E. coli cells cultivated at high osmotic pressure. Here, Q8 deficiency impaired E. coli growth at low osmotic pressure and rendered growth osmotically sensitive. The Q8 deficiency impeded cellular O2

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Sanders, M. R., H. E. Findlay та 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, № 8 (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 bacteri

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