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Volumn 77, Issue 13, 2011, Pages 4383-4389

Small-molecule inhibition of choline catabolism in Pseudomonas aeruginosa and other aerobic choline-catabolizing bacteria

Author keywords

[No Author keywords available]

Indexed keywords

A-CARBON; BIOINFORMATIC ANALYSIS; BURKHOLDERIA; BURKHOLDERIA CEPACIA; CHEMICAL INHIBITORS; DEMETHYLATION; DIMETHYLGLYCINE; ENERGY SOURCE; ENVIRONMENTAL ISOLATES; GENES ENCODING; GENETIC ANALYSIS; GROWTH INHIBITOR; IN-SITU; IN-VITRO; NUTRIENT CYCLING; P.AERUGINOSA; PROTEOBACTERIA; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS FLUORESCENS; PSEUDOMONAS MENDOCINA; PSEUDOMONAS PUTIDA; SINORHIZOBIUM MELILOTI; SMALL MOLECULES;

EID: 79960086955     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00504-11     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 33749644161 scopus 로고    scopus 로고
    • Interrelations between glycine betaine catabolism and methionine biosynthesis in Sinorhizobium meliloti strain 102F34
    • Barra, L., et al. 2006. Interrelations between glycine betaine catabolism and methionine biosynthesis in Sinorhizobium meliloti strain 102F34. J. Bacteriol. 188:7195-7204.
    • (2006) J. Bacteriol. , vol.188 , pp. 7195-7204
    • Barra, L.1
  • 2
    • 0017718999 scopus 로고
    • The characterisation of inducible dehydrogenases specific for the oxidation of D-alanine, allohydroxy-D-proline, choline and sarcosine as peripheral membrane proteins in Pseudomonas aeruginosa
    • Bater, A. J., and W. A. Venables. 1977. The characterisation of inducible dehydrogenases specific for the oxidation of D-alanine, allohydroxy-D-proline, choline and sarcosine as peripheral membrane proteins in Pseudomonas aeruginosa. Biochim. Biophys. Acta 468:209-226.
    • (1977) Biochim. Biophys. Acta. , vol.468 , pp. 209-226
    • Bater, A.J.1    Venables, W.A.2
  • 3
    • 12144289182 scopus 로고    scopus 로고
    • Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class
    • Binda, C., et al. 2004. Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J. Med. Chem. 47:1767-1774.
    • (2004) J. Med. Chem. , vol.47 , pp. 1767-1774
    • Binda, C.1
  • 4
    • 0028106108 scopus 로고
    • Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline
    • Boch, J., B. Kempf, and E. Bremer. 1994. Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline. J. Bacteriol. 176:5364-5371.
    • (1994) J. Bacteriol. , vol.176 , pp. 5364-5371
    • Boch, J.1    Kempf, B.2    Bremer, E.3
  • 5
    • 0032948078 scopus 로고    scopus 로고
    • Occurrence of choline and glycine betaine uptake and metabolism in the family Rhizobiaceae and their roles in osmoprotection
    • Boncompagni, E., M. Osteras, M. C. Poggi, and D. le Rudulier. 1999. Occurrence of choline and glycine betaine uptake and metabolism in the family Rhizobiaceae and their roles in osmoprotection. Appl. Environ. Microbiol. 65:2072-2077.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2072-2077
    • Boncompagni, E.1    Osteras, M.2    Poggi, M.C.3    le Rudulier, D.4
  • 6
    • 41949085567 scopus 로고    scopus 로고
    • Pseudomonas syringae BetT is a low-affinity choline transporter that is responsible for superior osmoprotection by choline over glycine betaine
    • Chen, C., and G. A. Beattie. 2008. Pseudomonas syringae BetT is a low-affinity choline transporter that is responsible for superior osmoprotection by choline over glycine betaine. J. Bacteriol. 190:2717-2725.
    • (2008) J. Bacteriol. , vol.190 , pp. 2717-2725
    • Chen, C.1    Beattie, G.A.2
  • 7
    • 72949101439 scopus 로고    scopus 로고
    • The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds
    • Chen, C., A. A. Malek, M. J. Wargo, D. A. Hogan, and G. A. Beattie. 2010. The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds. Mol. Microbiol. 75:29-45.
    • (2010) Mol. Microbiol. , vol.75 , pp. 29-45
    • Chen, C.1    Malek, A.A.2    Wargo, M.J.3    Hogan, D.A.4    Beattie, G.A.5
  • 8
    • 0029143934 scopus 로고
    • Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism
    • Chlumsky, L. J., L. Zhang, and M. S. Jorns. 1995. Sequence analysis of sarcosine oxidase and nearby genes reveals homologies with key enzymes of folate one-carbon metabolism. J. Biol. Chem. 270:18252-18259.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18252-18259
    • Chlumsky, L.J.1    Zhang, L.2    Jorns, M.S.3
  • 9
    • 32244448730 scopus 로고    scopus 로고
    • A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation
    • Choi, K.-H., A. Kumar, and H. P. Schweizer. 2006. A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation. J. Microbiol. Methods 64:391-397.
    • (2006) J. Microbiol. Methods. , vol.64 , pp. 391-397
    • Choi, K.-H.1    Kumar, A.2    Schweizer, H.P.3
  • 10
    • 0026006215 scopus 로고
    • Prokaryotic osmoregulation: genetics and physiology
    • Csonka, L. N., and A. D. Hanson. 1991. Prokaryotic osmoregulation: genetics and physiology. Annu. Rev. Microbiol. 45:569-606.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 569-606
    • Csonka, L.N.1    Hanson, A.D.2
  • 11
    • 33646767117 scopus 로고    scopus 로고
    • Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities
    • Diab, F., et al. 2006. Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities. Microbiology 152:1395-1406.
    • (2006) Microbiology , vol.152 , pp. 1395-1406
    • Diab, F.1
  • 12
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 13
    • 0017397471 scopus 로고
    • Further studies on the formation of choline sulfate by bacteria
    • Fitzgerald, J. W., and P. C. Luschinski. 1977. Further studies on the formation of choline sulfate by bacteria. Can. J. Microbiol. 23:483-490.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 483-490
    • Fitzgerald, J.W.1    Luschinski, P.C.2
  • 14
    • 45749124657 scopus 로고    scopus 로고
    • TNT, a free program for phylogenetic analysis
    • Goloboff, P. A., J. S. Farris, and K. C. Nixon. 2008. TNT, a free program for phylogenetic analysis. Cladistics 24:774-786.
    • (2008) Cladistics , vol.24 , pp. 774-786
    • Goloboff, P.A.1    Farris, J.S.2    Nixon, K.C.3
  • 15
    • 33344456354 scopus 로고    scopus 로고
    • Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine
    • Horn, C., et al. 2006. Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine. J. Mol. Biol. 357:592-606.
    • (2006) J. Mol. Biol. , vol.357 , pp. 592-606
    • Horn, C.1
  • 16
    • 0017666851 scopus 로고
    • Purification and characterization of choline oxidase from Arthrobacter globiformis
    • Ikuta, S., S. Imamura, H. Misaki, and Y. Horiuti. 1977. Purification and characterization of choline oxidase from Arthrobacter globiformis. J. Biochem. 82: 1741-1749.
    • (1977) J. Biochem. , vol.82 , pp. 1741-1749
    • Ikuta, S.1    Imamura, S.2    Misaki, H.3    Horiuti, Y.4
  • 17
    • 0034123698 scopus 로고    scopus 로고
    • Positive correlation between virulence of Pseudomonas aeruginosa mutants in mice and insects
    • Jander, G., L. G. Rahme, and F. M. Ausubel. 2000. Positive correlation between virulence of Pseudomonas aeruginosa mutants in mice and insects. J. Bacteriol. 182:3843-3845.
    • (2000) J. Bacteriol. , vol.182 , pp. 3843-3845
    • Jander, G.1    Rahme, L.G.2    Ausubel, F.M.3
  • 18
    • 70349342948 scopus 로고    scopus 로고
    • Metabolic labeling and direct imaging of choline phospholipids in vivo
    • Jao, C. Y., M. Roth, R. Welti, and A. Salic. 2009. Metabolic labeling and direct imaging of choline phospholipids in vivo. Proc. Natl. Acad. Sci. U. S. A. 106:15332-15337.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 15332-15337
    • Jao, C.Y.1    Roth, M.2    Welti, R.3    Salic, A.4
  • 19
    • 0029025354 scopus 로고
    • OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis
    • Kempf, B., and E. Bremer. 1995. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J. Biol. Chem. 270:16701-16713.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16701-16713
    • Kempf, B.1    Bremer, E.2
  • 20
    • 0014723017 scopus 로고
    • The aerobic decomposition of choline by microorganisms. I. The ability of aerobic organisms, particularly coryneform bacteria, to utilize choline as the sole carbon and nitrogen source
    • Kortstee, G. J. 1970. The aerobic decomposition of choline by microorganisms. I. The ability of aerobic organisms, particularly coryneform bacteria, to utilize choline as the sole carbon and nitrogen source. Arch. Mikrobiol. 71:235-244.
    • (1970) Arch. Mikrobiol. , vol.71 , pp. 235-244
    • Kortstee, G.J.1
  • 21
    • 0016771564 scopus 로고
    • Role of the substituants N-allyl and N-propargyl on the mechanism of flavoprotein enzyme inhibition: N-demethylase and monoamineoxidase
    • Kraus, J.-L., J.-J. Yaouanc, and G. Sturtz. 1975. Role of the substituants N-allyl and N-propargyl on the mechanism of flavoprotein enzyme inhibition: N-demethylase and monoamineoxidase. Eur. J. Med. Chem. 10:507-513.
    • (1975) Eur. J. Med. Chem. , vol.10 , pp. 507-513
    • Kraus, J.-L.1    Yaouanc, J.-J.2    Sturtz, G.3
  • 22
    • 0022503080 scopus 로고
    • Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli
    • Landfald, B., and A. R. Strom. 1986. Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli. J. Bacteriol. 165: 849-855.
    • (1986) J. Bacteriol. , vol.165 , pp. 849-855
    • Landfald, B.1    Strom, A.R.2
  • 24
    • 79958052128 scopus 로고    scopus 로고
    • Roles of three transporters, CbcXWV, BetT1, and BetT3, in Pseudomonas aeruginosa choline uptake for catabolism
    • 8 April. doi:10.1128/JB.00160-11
    • Malek, A. A., C. Chen, M. J. Wargo, G. A. Beattie, and D. A. Hogan. 8 April 2011. Roles of three transporters, CbcXWV, BetT1, and BetT3, in Pseudomonas aeruginosa choline uptake for catabolism. J. Bacteriol. doi:10.1128/JB.00160-11.
    • (2011) J. Bacteriol
    • Malek, A.A.1    Chen, C.2    Wargo, M.J.3    Beattie, G.A.4    Hogan, D.A.5
  • 25
    • 0034832015 scopus 로고    scopus 로고
    • Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp : implications for glycine betaine catabolism
    • Meskys, R., R. J. Harris, V. Casaite, J. Basran, and N. S. Scrutton. 2001. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268:3390-3398.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3390-3398
    • Meskys, R.1    Harris, R.J.2    Casaite, V.3    Basran, J.4    Scrutton, N.S.5
  • 28
    • 34249864455 scopus 로고    scopus 로고
    • Clinical response to azithromycin in cystic fibrosis correlates with in vitro effects on Pseudomonas aeruginosa phenotypes
    • Nguyen, D., et al. 2007. Clinical response to azithromycin in cystic fibrosis correlates with in vitro effects on Pseudomonas aeruginosa phenotypes. Pediatr. Pulmonol. 42:533-541.
    • (2007) Pediatr. Pulmonol. , vol.42 , pp. 533-541
    • Nguyen, D.1
  • 29
    • 0023612039 scopus 로고
    • Identification of a new phospholipase C activity by analysis of an insertional mutation in the hemolytic phospholipase C structural gene of Pseudomonas aeruginosa
    • Ostroff, R. M., and M. L. Vasil. 1987. Identification of a new phospholipase C activity by analysis of an insertional mutation in the hemolytic phospholipase C structural gene of Pseudomonas aeruginosa. J. Bacteriol. 169:4597-4601.
    • (1987) J. Bacteriol. , vol.169 , pp. 4597-4601
    • Ostroff, R.M.1    Vasil, M.L.2
  • 30
    • 0029035765 scopus 로고
    • Common virulence factors for bacterial pathogenicity in plants and animals
    • Rahme, L. G., et al. 1995. Common virulence factors for bacterial pathogenicity in plants and animals. Science 268:1899-1902.
    • (1995) Science , vol.268 , pp. 1899-1902
    • Rahme, L.G.1
  • 31
    • 0028191244 scopus 로고
    • Choline-O-sulfate biosynthesis in plants (identification and partial characterization of a salinity-inducible choline sulfotransferase from species of Limonium (Plumbaginaceae)
    • Rivoal, J., and A. D. Hanson. 1994. Choline-O-sulfate biosynthesis in plants (identification and partial characterization of a salinity-inducible choline sulfotransferase from species of Limonium (Plumbaginaceae). Plant Physiol. 106:1187-1193.
    • (1994) Plant Physiol , vol.106 , pp. 1187-1193
    • Rivoal, J.1    Hanson, A.D.2
  • 32
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist, F., and J. P. Huelsenbeck. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 33
    • 0031032631 scopus 로고    scopus 로고
    • Molecular characterization of mutants affected in the osmoprotectant-dependent induction of phospholipase C in Pseudomonas aeruginosa PAO1
    • Sage, A. E., A. I. Vasil, and M. L. Vasil. 1997. Molecular characterization of mutants affected in the osmoprotectant-dependent induction of phospholipase C in Pseudomonas aeruginosa PAO1. Mol. Microbiol. 23:43-56.
    • (1997) Mol. Microbiol. , vol.23 , pp. 43-56
    • Sage, A.E.1    Vasil, A.I.2    Vasil, M.L.3
  • 34
    • 0027134384 scopus 로고
    • Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis
    • Schweizer, H. D. 1993. Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis. Biotechniques 15:831-834.
    • (1993) Biotechniques , vol.15 , pp. 831-834
    • Schweizer, H.D.1
  • 35
    • 33746045692 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria
    • Shanks, R. M., N. C. Caiazza, S. M. Hinsa, C. M. Toutain, and G. A. O'Toole. 2006. Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria. Appl. Environ. Microbiol. 72:5027-5036.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5027-5036
    • Shanks, R.M.1    Caiazza, N.C.2    Hinsa, S.M.3    Toutain, C.M.4    O'Toole, G.A.5
  • 36
    • 0026576479 scopus 로고
    • Osmoprotectants and phosphate regulate expression of phospholipase C in Pseudomonas aeruginosa
    • Shortridge, V. D., A. Lazdunski, and M. L. Vasil. 1992. Osmoprotectants and phosphate regulate expression of phospholipase C in Pseudomonas aeruginosa. Mol. Microbiol. 6:863-871.
    • (1992) Mol. Microbiol. , vol.6 , pp. 863-871
    • Shortridge, V.D.1    Lazdunski, A.2    Vasil, M.L.3
  • 37
    • 0034957644 scopus 로고    scopus 로고
    • Purification and kinetic properties of betaine-homocysteine methyltransferase from Aphanothece halophytica
    • Waditee, R., and A. Incharoensakdi. 2001. Purification and kinetic properties of betaine-homocysteine methyltransferase from Aphanothece halophytica. Curr. Microbiol. 43:107-111.
    • (2001) Curr. Microbiol. , vol.43 , pp. 107-111
    • Waditee, R.1    Incharoensakdi, A.2
  • 38
    • 0033609040 scopus 로고    scopus 로고
    • Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase
    • Wagner, M. A., P. Khanna, and M. S. Jorns. 1999. Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase. Biochemistry 38:5588-5595.
    • (1999) Biochemistry , vol.38 , pp. 5588-5595
    • Wagner, M.A.1    Khanna, P.2    Jorns, M.S.3
  • 39
    • 0015523668 scopus 로고
    • Inactivation of a flavoprotein, lactate oxidase, by an acetylenic substrate
    • Walsh, C. T., A. Schonbrunn, O. Lockridge, V. Massey, and R. H. Abeles. 1972. Inactivation of a flavoprotein, lactate oxidase, by an acetylenic substrate. J. Biol. Chem. 247:6004-6006.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6004-6006
    • Walsh, C.T.1    Schonbrunn, A.2    Lockridge, O.3    Massey, V.4    Abeles, R.H.5
  • 40
    • 62449310633 scopus 로고    scopus 로고
    • GbdR regulates Pseudomonas aeruginosa plcH and pchP transcription in response to choline catabolites
    • Wargo, M. J., T. C. Ho, M. J. Gross, L. A. Whittaker, and D. A. Hogan. 2009. GbdR regulates Pseudomonas aeruginosa plcH and pchP transcription in response to choline catabolites. Infect. Immun. 77:1103-1111.
    • (2009) Infect. Immun. , vol.77 , pp. 1103-1111
    • Wargo, M.J.1    Ho, T.C.2    Gross, M.J.3    Whittaker, L.A.4    Hogan, D.A.5
  • 41
    • 69949147631 scopus 로고    scopus 로고
    • Identification of genes required for Pseudomonas aeruginosa carnitine catabolism
    • Wargo, M. J., and D. A. Hogan. 2009. Identification of genes required for Pseudomonas aeruginosa carnitine catabolism. Microbiology 155:2411-2419.
    • (2009) Microbiology , vol.155 , pp. 2411-2419
    • Wargo, M.J.1    Hogan, D.A.2
  • 42
    • 41949101593 scopus 로고    scopus 로고
    • Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism
    • Wargo, M. J., B. S. Szwergold, and D. A. Hogan. 2008. Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism. J. Bacteriol. 190:2690-2699.
    • (2008) J. Bacteriol. , vol.190 , pp. 2690-2699
    • Wargo, M.J.1    Szwergold, B.S.2    Hogan, D.A.3
  • 43
    • 0027491593 scopus 로고
    • Alveolar epithelial injury and pleural empyema in acute P. aeruginosa pneumonia in anesthetized rabbits
    • Wiener-Kronish, J. P., et al. 1993. Alveolar epithelial injury and pleural empyema in acute P. aeruginosa pneumonia in anesthetized rabbits. J. Appl. Physiol. 75:1661-1669.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1661-1669
    • Wiener-Kronish, J.P.1
  • 44
    • 0029913243 scopus 로고    scopus 로고
    • Sarcosine oxidase contains a novel covalently bound FMN
    • Willie, A., D. E. Edmondson, and M. S. Jorns. 1996. Sarcosine oxidase contains a novel covalently bound FMN. Biochemistry 35:5292-5299.
    • (1996) Biochemistry , vol.35 , pp. 5292-5299
    • Willie, A.1    Edmondson, D.E.2    Jorns, M.S.3
  • 45
    • 35748942898 scopus 로고    scopus 로고
    • Bacterial osmosensing transporters
    • Wood, J. M. 2007. Bacterial osmosensing transporters. Methods Enzymol. 428:77-107.
    • (2007) Methods Enzymol , vol.428 , pp. 77-107
    • Wood, J.M.1
  • 46
    • 0025151131 scopus 로고
    • Choline deficiency
    • Zeisel, S. H. 1990. Choline deficiency. J. Nutr. Biochem. 1:332-349.
    • (1990) J. Nutr. Biochem. , vol.1 , pp. 332-349
    • Zeisel, S.H.1
  • 47
    • 77957234040 scopus 로고    scopus 로고
    • The BCCT family of carriers: from physiology to crystal structure
    • Ziegler, C., E. Bremer, and R. Kramer. 2010. The BCCT family of carriers: from physiology to crystal structure. Mol. Microbiol. 78:13-34.
    • (2010) Mol. Microbiol. , vol.78 , pp. 13-34
    • Ziegler, C.1    Bremer, E.2    Kramer, R.3


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