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Journal articles on the topic 'Oligopeptides transport systems'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Chothe, Paresh, Nagendra Singh, and Vadivel Ganapathy. "Evidence for two different broad-specificity oligopeptide transporters in intestinal cell line Caco-2 and colonic cell line CCD841." American Journal of Physiology-Cell Physiology 300, no. 6 (2011): C1260—C1269. http://dx.doi.org/10.1152/ajpcell.00299.2010.

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Recently the existence of two different Na+-coupled oligopeptide transport systems has been described in mammalian cells. These transport systems are distinct from the previously known H+/peptide cotransporters PEPT1 and PEPT2, which transport only dipeptides and tripeptides. To date, the only peptide transport system known to exist in the intestine is PEPT1. Here we investigated the expression of the Na+-coupled oligopeptide transporters in intestinal cell lines, using the hydrolysis-resistant synthetic oligopeptides deltorphin II and [d-Ala2,d-Leu5]enkephalin (DADLE) as model substrates. Cac

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2

Verheul, Annette, Frank M. Rombouts, and Tjakko Abee. "Utilization of Oligopeptides by Listeria monocytogenes Scott A." Applied and Environmental Microbiology 64, no. 3 (1998): 1059–65. http://dx.doi.org/10.1128/aem.64.3.1059-1065.1998.

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ABSTRACT For effective utilization of peptides, Listeria monocytogenes possesses two different peptide transport systems. The first one is the previously described proton motive force (PMF)-driven di- and tripeptide transport system (A. Verheul, A. Hagting, M.-R. Amezaga, I. R. Booth, F. M. Rombouts, and T. Abee, Appl. Environ. Microbiol. 61:226–233, 1995). The present results reveal that L. monocytogenes possesses an oligopeptide transport system, presumably requiring ATP rather than the PMF as the driving force for translocation. Experiments to determine growth in a defined medium containing

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3

Hiron, Aurelia, Elise Borezée-Durant, Jean-Christophe Piard, and Vincent Juillard. "Only One of Four Oligopeptide Transport Systems Mediates Nitrogen Nutrition in Staphylococcus aureus." Journal of Bacteriology 189, no. 14 (2007): 5119–29. http://dx.doi.org/10.1128/jb.00274-07.

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ABSTRACT Oligopeptides internalized by oligopeptide permease (Opp) transporters play key roles in bacterial nutrition, signaling, and virulence. To date, two opp operons, opp-1 and opp-2, have been identified in Staphylococcus aureus. Systematic in silico analysis of 11 different S. aureus genomes revealed the existence of two new opp operons, opp-3 and opp-4, plus an opp-5A gene encoding a putative peptide-binding protein. With the exception of opp-4, the opp operons were present in all S. aureus strains. Within a single strain, the different opp operons displayed little sequence similarity a

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4

Wiles, Amy M., Houjian Cai, Fred Naider, and Jeffrey M. Becker. "Nutrient regulation of oligopeptide transport in Saccharomyces cerevisiae." Microbiology 152, no. 10 (2006): 3133–45. http://dx.doi.org/10.1099/mic.0.29055-0.

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Small peptides (2–5 amino acid residues) are transported into Saccharomyces cerevisiae via two transport systems: PTR (Peptide TRansport) for di-/tripeptides and OPT (OligoPeptide Transport) for oligopeptides of 4–5 amino acids in length. Although regulation of the PTR system has been studied in some detail, neither the regulation of the OPT family nor the environmental conditions under which family members are normally expressed have been well studied in S. cerevisiae. Using a lacZ reporter gene construct fused to 1 kb DNA from upstream of the genes OPT1 and OPT2, which encode the two S. cere

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5

Minami, H., H. Daniel, E. L. Morse, and S. A. Adibi. "Oligopeptides: mechanism of renal clearance depends on molecular structure." American Journal of Physiology-Renal Physiology 263, no. 1 (1992): F109—F115. http://dx.doi.org/10.1152/ajprenal.1992.263.1.f109.

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We have investigated the relative contribution of hydrolysis, intact transport and urinary excretion to the renal clearance of Gly-Sar, Gly-Sar-Sar, and Gly-Gly-Sar in fed and starved rats. The results obtained from isolated kidney perfusion studies are summarized as follows: 1) clearance was fastest for Gly-Gly-Sar and slowest for Gly-Sar-Sar, 2) urinary excretion of Gly-Sar-Sar exceeded that of Gly-Gly-Sar or Gly-Sar, 3) there was accumulation of products of hydrolysis of Gly-Gly-Sar in the perfusate but not of Gly-Sar or Gly-Sar-Sar, 4) isolated brush-border and basolateral membranes of ren

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6

Koide, Akiko, Marta Perego, and James A. Hoch. "ScoC Regulates Peptide Transport and Sporulation Initiation in Bacillus subtilis." Journal of Bacteriology 181, no. 13 (1999): 4114–17. http://dx.doi.org/10.1128/jb.181.13.4114-4117.1999.

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ABSTRACT Oligopeptides are transported into Bacillus subtilis by two ABC transport systems, App and Opp. Transcription of the operon encoding the Opp system was found to occur during exponential growth, whereas the app operon was induced at the onset of stationary phase. Transcription of both operons was completely curtailed by overproduction of the ScoC regulator from a multicopy plasmid and was enhanced in strains with the scoC locus deleted. ScoC, a member of the MarR family of transcription regulators, is known from previous studies to be a negative regulator of sporulation and of protease

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7

Daniel, Hannelore, and Isabel Rubio-Aliaga. "An update on renal peptide transporters." American Journal of Physiology-Renal Physiology 284, no. 5 (2003): F885—F892. http://dx.doi.org/10.1152/ajprenal.00123.2002.

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The brush-border membrane of renal epithelial cells contains PEPT1 and PEPT2 proteins that are rheogenic carriers for short-chain peptides. The carrier proteins display a distinct surface expression pattern along the proximal tubule, suggesting that initially di- and tripeptides, either filtered or released by surface-bound hydrolases from larger oligopeptides, are taken up by the low-affinity but high-capacity PEPT1 transporter and then by PEPT2, which possesses a higher affinity but lower transport capacity. Both carriers transport essentially all possible di- and tripeptides and numerous st

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8

Weinberg, Michael V., and Robert J. Maier. "Peptide Transport in Helicobacter pylori: Roles of Dpp and Opp Systems and Evidence for Additional Peptide Transporters." Journal of Bacteriology 189, no. 9 (2007): 3392–402. http://dx.doi.org/10.1128/jb.01636-06.

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ABSTRACT Despite research into the nutritional requirements of Helicobacter pylori, little is known regarding its use of complex substrates, such as peptides. Analysis of genome sequences revealed putative ABC-type transporter genes for dipeptide (dppABCDF) and oligopeptide (oppABCD) transport. Genes from each system were PCR amplified, cloned, and disrupted by cassette insertion either individually (dppA, dppB, dppC, oppA, oppB, and oppC) or to create double mutants (dppA oppA, dppB oppB, dppB dppC, and oppB oppC). Peptide-utilizing abilities of the strains were assessed by monitoring growth

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9

Dunkel, Nico, Tobias Hertlein, Renate Franz, et al. "Roles of Different Peptide Transporters in Nutrient Acquisition in Candida albicans." Eukaryotic Cell 12, no. 4 (2013): 520–28. http://dx.doi.org/10.1128/ec.00008-13.

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ABSTRACT Fungi possess two distinct proton-coupled peptide transport systems, the dipeptide/tripeptide transporters (PTR) and the oligopeptide transporters (OPT), which enable them to utilize peptides as nutrients. In the pathogenic yeast Candida albicans , peptide transporters are encoded by gene families consisting of two PTR genes and eight OPT genes. To gain insight into the functions and importance of specific peptide transporters, we generated mutants lacking the two dipeptide/tripeptide transporters Ptr2 and Ptr22, as well as the five major oligopeptide transporters Opt1 to Opt5. These

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10

Picon, A., M. A. García-Casado, and M. Nuñez. "Proteolytic activities, peptide utilization and oligopeptide transport systems of wild Lactococcus lactis strains." International Dairy Journal 20, no. 3 (2010): 156–62. http://dx.doi.org/10.1016/j.idairyj.2009.10.002.

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11

Conners, Shannon B., Clemente I. Montero, Donald A. Comfort, et al. "An Expression-Driven Approach to the Prediction of Carbohydrate Transport and Utilization Regulons in theHyperthermophilic Bacterium Thermotoga maritima." Journal of Bacteriology 187, no. 21 (2005): 7267–82. http://dx.doi.org/10.1128/jb.187.21.7267-7282.2005.

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ABSTRACT Comprehensive analysis of genome-wide expression patterns during growth of the hyperthermophilic bacterium Thermotoga maritima on 14 monosaccharide and polysaccharide substrates was undertaken with the goal of proposing carbohydrate specificities for transport systems and putative transcriptional regulators. Saccharide-induced regulons were predicted through the complementary use of comparative genomics, mixed-model analysis of genome-wide microarray expression data, and examination of upstream sequence patterns. The results indicate that T. maritima relies extensively on ABC transpor

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12

Gardan, Rozenn, Colette Besset, Alain Guillot, Christophe Gitton, and Véronique Monnet. "The Oligopeptide Transport System Is Essential for the Development of Natural Competence in Streptococcus thermophilus Strain LMD-9." Journal of Bacteriology 191, no. 14 (2009): 4647–55. http://dx.doi.org/10.1128/jb.00257-09.

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ABSTRACT In gram-positive bacteria, oligopeptide transport systems, called Opp or Ami, play a role in nutrition but are also involved in the internalization of signaling peptides that take part in the functioning of quorum-sensing pathways. Our objective was to reveal functions that are controlled by Ami via quorum-sensing mechanisms in Streptococcus thermophilus, a nonpathogenic bacterium widely used in dairy technology in association with other bacteria. Using a label-free proteomic approach combining one-dimensional electrophoresis with liquid chromatography-tandem mass spectrometry analysi

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13

Buurman, Ed T., Debbie McLaggan, Josef Naprstek, and Wolfgang Epstein. "Multiple Paths for Nonphysiological Transport of K+ in Escherichia coli." Journal of Bacteriology 186, no. 13 (2004): 4238–45. http://dx.doi.org/10.1128/jb.186.13.4238-4245.2004.

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ABSTRACT Mutants of Escherichia coli lacking all of the known saturable K+ transport systems, “triple mutants,” require elevated K+ concentrations for growth. K+ transport activity in such mutants, called TrkF activity, has low substrate specificity and a low rate that increases with increasing external pH. Attempts to isolate mutants requiring even higher concentrations of K+ failed, implying that either TrkF is essential or is composed of multiple minor K+ transport activities. Instead, we sought mutations that allowed triple mutants to grow at lower K+ concentrations. Mutations so identifie

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14

Urbanowski, Mark L., Lorraine T. Stauffer, and George V. Stauffer. "ThegcvBgene encodes a small untranslated RNA involved in expression of the dipeptide and oligopeptide transport systems inEscherichia coli." Molecular Microbiology 37, no. 4 (2000): 856–68. http://dx.doi.org/10.1046/j.1365-2958.2000.02051.x.

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15

Hebert, Elvira M., Graciela S. De Giori, and Raul R. Raya. "Isolation and Characterization of a Slowly Milk-Coagulating Variant of Lactobacillus helveticus Deficient in Purine Biosynthesis." Applied and Environmental Microbiology 67, no. 4 (2001): 1846–50. http://dx.doi.org/10.1128/aem.67.4.1846-1850.2001.

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ABSTRACT A slowly milk-coagulating variant (Fmc−) ofLactobacillus helveticus CRL 1062, designated S1, was isolated and characterized. Strain S1 possessed all the known essential components required to utilize casein as a nitrogen source, which include functional proteinase and peptidase activities as well as functional amino acid, di- and tripeptide, and oligopeptide transport systems. The amino acid requirements of strain S1 were similar to those of the parental strain. However, on a purine-free, chemically defined medium, the growth rate of the Fmc− strain was threefold lower than that of th

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16

Azcarate-Peril, M. Andrea, Olivia McAuliffe, Eric Altermann, Sonja Lick, W. Michael Russell, and Todd R. Klaenhammer. "Microarray Analysis of a Two-Component Regulatory System Involved in Acid Resistance and Proteolytic Activity in Lactobacillus acidophilus." Applied and Environmental Microbiology 71, no. 10 (2005): 5794–804. http://dx.doi.org/10.1128/aem.71.10.5794-5804.2005.

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ABSTRACT Two-component regulatory systems are one primary mechanism for environmental sensing and signal transduction. Annotation of the complete genome sequence of the probiotic bacterium Lactobacillus acidophilus NCFM revealed nine two-component regulatory systems. In this study, the histidine protein kinase of a two-component regulatory system (LBA1524HPK-LBA1525RR), similar to the acid-related system lisRK from Listeria monocytogenes (P. D. Cotter et al., J. Bacteriol. 181:6840-6843, 1999), was insertionally inactivated. A whole-genome microarray containing 97.4% of the annotated genes of

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17

Pulvermacher, Sarah C., Lorraine T. Stauffer, and George V. Stauffer. "The Small RNA GcvB Regulates sstT mRNA Expression in Escherichia coli." Journal of Bacteriology 191, no. 1 (2008): 238–48. http://dx.doi.org/10.1128/jb.00915-08.

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ABSTRACT In Escherichia coli, the gcvB gene encodes a nontranslated RNA (referred to as GcvB) that regulates OppA and DppA, two periplasmic binding proteins for the oligopeptide and dipeptide transport systems. An additional regulatory target of GcvB, sstT, was found by microarray analysis of RNA isolated from a wild-type strain and a gcvB deletion strain grown to mid-log phase in Luria-Bertani broth. The SstT protein functions to transport l-serine and l-threonine by sodium transport into the cell. Reverse transcription-PCR and translational fusions confirmed that GcvB negatively regulates ss

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18

Wang, Hua, Weizhu Yu, Tim Coolbear, Dan O’Sullivan, and Larry L. McKay. "A Deficiency in Aspartate Biosynthesis inLactococcus lactis subsp. lactis C2 Causes Slow Milk Coagulation." Applied and Environmental Microbiology 64, no. 5 (1998): 1673–79. http://dx.doi.org/10.1128/aem.64.5.1673-1679.1998.

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ABSTRACT A mutant of fast milk-coagulating (Fmc+)Lactococcus lactis subsp. lactis C2, designatedL. lactis KB4, was identified. Although possessing the known components essential for utilizing casein as a nitrogen source, which include functional proteinase (PrtP) activity and oligopeptide, di- and tripeptide, and amino acid transport systems, KB4 exhibited a slow milk coagulation (Fmc−) phenotype. When the amino acid requirements of L. lactis C2 were compared with those of KB4 by use of a chemically defined medium, it was found that KB4 was unable to grow in the absence of aspartic acid. This

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19

Pulvermacher, Sarah C., Lorraine T. Stauffer, and George V. Stauffer. "Role of the Escherichia coli Hfq protein in GcvB regulation of oppA and dppA mRNAs." Microbiology 155, no. 1 (2009): 115–23. http://dx.doi.org/10.1099/mic.0.023432-0.

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The gcvB gene encodes a small non-translated RNA (referred to as GcvB) that regulates oppA and dppA, two genes that encode periplasmic binding proteins for the oligopeptide and dipeptide transport systems. Hfq, an RNA chaperone protein, binds many small RNAs and is required for the small RNAs to regulate expression of their respective target genes. We showed that repression by GcvB of dppA : : lacZ and oppA : : phoA translational fusions is dependent upon Hfq. Double mutations in gcvB and hfq yielded similar expression levels of dppA : : lacZ and oppA : : phoA compared with gcvB or hfq single

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20

Lu, Chung-Dar, Zhe Yang, and Wei Li. "Transcriptome Analysis of the ArgR Regulon in Pseudomonas aeruginosa." Journal of Bacteriology 186, no. 12 (2004): 3855–61. http://dx.doi.org/10.1128/jb.186.12.3855-3861.2004.

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ABSTRACT Arginine metabolism in pseudomonads with multiple catabolic pathways for its utilization as carbon and nitrogen sources is of particular interest as the model system to study control of metabolic integration. We performed transcriptome analyses to identify genes controlled by the arginine regulatory protein ArgR and to better understand arginine metabolic pathways of P. aeruginosa. We compared gene expression in wild-type strain PAO1 with that in argR mutant strain PAO501 grown in glutamate minimal medium in the presence and absence of arginine. Ten putative transcriptional units of 2

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21

Yu, Yanbao, Tamara Tsitrin, Shiferaw Bekele, et al. "Aerococcus urinae and Globicatella sanguinis Persist in Polymicrobial Urethral Catheter Biofilms Examined in Longitudinal Profiles at the Proteomic Level." Biochemistry Insights 12 (January 2019): 117862641987508. http://dx.doi.org/10.1177/1178626419875089.

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Aerococcus urinae ( Au) and Globicatella sanguinis ( Gs) are gram-positive bacteria belonging to the family Aerococcaceae and colonize the human immunocompromised and catheterized urinary tract. We identified both pathogens in polymicrobial urethral catheter biofilms (CBs) with a combination of 16S rDNA sequencing, proteomic analyses, and microbial cultures. Longitudinal sampling of biofilms from serially replaced catheters revealed that each species persisted in the urinary tract of a patient in cohabitation with 1 or more gram-negative uropathogens. The Gs and Au proteomes revealed active gl

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22

Ge, Yixin, Jae Hoon Lee, Baishi Hu, and Youfu Zhao. "Loss-of-Function Mutations in the Dpp and Opp Permeases Render Erwinia amylovora Resistant to Kasugamycin and Blasticidin S." Molecular Plant-Microbe Interactions® 31, no. 8 (2018): 823–32. http://dx.doi.org/10.1094/mpmi-01-18-0007-r.

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Extensive use of the antibiotic streptomycin to control fire blight disease of apples and pears, caused by the enterobacterial plant pathogen Erwinia amylovora, leads to the development of streptomycin-resistant strains in the United States and elsewhere. Kasugamycin (Ksg) has been permitted to be used as an alternative or replacement to control this serious bacterial disease. In this study, we investigated the role of two major peptide ATP-binding cassette transporter systems in E. amylovora, the dipeptide permease (Dpp) and oligopeptide permease (Opp), in conferring sensitivity to Ksg and bl

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23

Pletzer, Daniel, Yvonne Braun, Svetlana Dubiley, et al. "The Pseudomonas aeruginosa PA14 ABC Transporter NppA1A2BCD Is Required for Uptake of Peptidyl Nucleoside Antibiotics." Journal of Bacteriology 197, no. 13 (2015): 2217–28. http://dx.doi.org/10.1128/jb.00234-15.

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ABSTRACTAnalysis of the genome sequence ofPseudomonas aeruginosaPA14 revealed the presence of an operon encoding an ABC-type transporter (NppA1A2BCD) showing homology to the Yej transporter ofEscherichia coli. The Yej transporter is involved in the uptake of the peptide-nucleotide antibiotic microcin C, a translation inhibitor that targets the enzyme aspartyl-tRNA synthetase. Furthermore, it was recently shown that the Opp transporter fromP. aeruginosaPAO1, which is identical to Npp, is required for uptake of the uridyl peptide antibiotic pacidamycin, which targets the enzyme translocase I (Mr

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24

Liang, Huihui, Yinting Mao, Yijuan Sun, and Haichun Gao. "Transcriptional regulator ArcA mediates expression of oligopeptide transport systems both directly and indirectly in Shewanella oneidensis." Scientific Reports 9, no. 1 (2019). http://dx.doi.org/10.1038/s41598-019-50201-4.

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Abstract In γ-proteobacterial species, such as Escherichia coli, the Arc (anoxic redox control) two-component system plays a major role in mediating the metabolic transition from aerobiosis to anaerobiosis, and thus is crucial for anaerobic growth but dispensable for aerobic growth. In Shewanella oneidensis, a bacterium renowned for respiratory versatility, Arc (SoArc) primarily affects aerobic growth. To date, how this occurs has remained largely unknown although the growth defect resulting from the loss of DNA-binding response regulator SoArcA is tryptone-dependent. In this study, we demonst

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25

Kramer, Werner. "Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery." Biological Chemistry 392, no. 1-2 (2011). http://dx.doi.org/10.1515/bc.2011.017.

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Abstract Membrane transporters are major determinants for the pharmacokinetic, safety and efficacy behavior of drugs. Available technologies to study function and structure of transport proteins has strongly stimulated research in transporter biology and uncovered their importance for the drug discovery and development process, especially for drug absorption and disposition. Physiological transport systems are investigated as potential ferries to improve drug absorption and membrane permeation and to achieve organ-specific drug action. In particular, the bile acid transport systems in the live

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26

Álvarez-Álvarez, R., A. Rodríguez-García, Y. Martínez-Burgo, J. F. Martín, and P. Liras. "Transcriptional Studies on aStreptomyces clavuligerus oppA2Deletion Mutant:N-Acetylglycyl-Clavaminic Acid Is an Intermediate of Clavulanic Acid Biosynthesis." Applied and Environmental Microbiology 84, no. 22 (2018). http://dx.doi.org/10.1128/aem.01701-18.

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ABSTRACTTheoppA2gene encodes an oligopeptide-binding protein similar to the periplasmic substrate-binding proteins of the ABC transport systems. However,oppA2is an orphan gene, not included in an ABC operon. This gene is located in the clavulanic acid (CA) gene cluster ofStreptomyces clavuligerusand is essential for CA production. A transcriptomic study of theoppA2-null mutantS. clavuligerusΔoppA2::aacshowed changes in the expression levels of 233 genes from those in the parental strain. These include genes for ABC transport systems, secreted proteins, peptidases, and proteases. Expression of

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