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Volumn 13, Issue 2, 2007, Pages 74-82

Isolation and characterization of the Omp-PA porin from Porphyromonas asaccharolytica, determination of the omp-PA gene sequence and prediction of Omp-PA protein structure

Author keywords

"Closed" conformer; "Open" conformer; Outer membrane protein; Porin; Porphyromonas asaccharolytica

Indexed keywords

LIPOSOME; OUTER MEMBRANE PROTEIN; PORIN; SUGAR;

EID: 34347256778     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.anaerobe.2006.11.003     Document Type: Article
Times cited : (4)

References (38)
  • 1
    • 34347227666 scopus 로고    scopus 로고
    • Jousimies-Somer H., Summanen P., Citron D., Baron E., Wexler H., and Finegold S. (Eds), Star Publishing Company, Belmont, CA (Chapter 6)
    • In: Jousimies-Somer H., Summanen P., Citron D., Baron E., Wexler H., and Finegold S. (Eds). Wadsworth-KTL anaerobic bacteriology manual. 6th ed (2002), Star Publishing Company, Belmont, CA 92-98 (Chapter 6)
    • (2002) Wadsworth-KTL anaerobic bacteriology manual. 6th ed , pp. 92-98
  • 2
    • 0033991475 scopus 로고    scopus 로고
    • Outer-membrane proteins pattern and detection of beta-lactamases in clinical isolates of imipenem-resistant Acinetobacter baumannii from Brazil
    • Costa S., Woodcock J., Gill M., Wise R., Barone A., Caiaffa H., et al. Outer-membrane proteins pattern and detection of beta-lactamases in clinical isolates of imipenem-resistant Acinetobacter baumannii from Brazil. Int J Antimicrob Agents 13 (2000) 175-182
    • (2000) Int J Antimicrob Agents , vol.13 , pp. 175-182
    • Costa, S.1    Woodcock, J.2    Gill, M.3    Wise, R.4    Barone, A.5    Caiaffa, H.6
  • 3
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol Microbiol 16 (1995) 1269-1270
    • (1995) Mol Microbiol , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 4
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang Y. The function of OmpA in Escherichia coli. Biochem Biophys Res Commun 292 (2002) 396-401
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 396-401
    • Wang, Y.1
  • 5
    • 0036385747 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F is an adhesin in bacterial binding to lung epithelial cells in culture
    • Azghani A., Idell S., Bains M., and Hancock R. Pseudomonas aeruginosa outer membrane protein F is an adhesin in bacterial binding to lung epithelial cells in culture. Microb Pathog 33 (2002) 109-114
    • (2002) Microb Pathog , vol.33 , pp. 109-114
    • Azghani, A.1    Idell, S.2    Bains, M.3    Hancock, R.4
  • 6
    • 0033828880 scopus 로고    scopus 로고
    • Role of porin of Shigella dysenteriae type 1 in modulation of lipopolysaccharide mediated nitric oxide and interleukin-1 release by murine peritoneal macrophages
    • Biswas T. Role of porin of Shigella dysenteriae type 1 in modulation of lipopolysaccharide mediated nitric oxide and interleukin-1 release by murine peritoneal macrophages. FEMS Immunol Med Microbiol 29 (2000) 129-136
    • (2000) FEMS Immunol Med Microbiol , vol.29 , pp. 129-136
    • Biswas, T.1
  • 7
    • 0030953947 scopus 로고    scopus 로고
    • Porins of Pseudomonas aeruginosa induce release of tumor necrosis factor alpha and interleukin-6 by human leukocytes
    • Cusumano V., Tufano M., Mancuso G., Carbone M., Rossano F., Fera M., et al. Porins of Pseudomonas aeruginosa induce release of tumor necrosis factor alpha and interleukin-6 by human leukocytes. Infect Immun 65 (1997) 1683-1687
    • (1997) Infect Immun , vol.65 , pp. 1683-1687
    • Cusumano, V.1    Tufano, M.2    Mancuso, G.3    Carbone, M.4    Rossano, F.5    Fera, M.6
  • 9
    • 0024501638 scopus 로고
    • Role of protein F in maintaining structural integrity of the Pseudomonas aeruginosa outer membrane
    • Gotoh N., Wakebe H., Yoshihara E., Nakae T., and Nishino T. Role of protein F in maintaining structural integrity of the Pseudomonas aeruginosa outer membrane. J Bacteriol 171 (1989) 983-990
    • (1989) J Bacteriol , vol.171 , pp. 983-990
    • Gotoh, N.1    Wakebe, H.2    Yoshihara, E.3    Nakae, T.4    Nishino, T.5
  • 10
    • 0017037714 scopus 로고
    • Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12
    • Nakamura K., and Mizushima S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J Biochem (Tokyo) 80 (1976) 1411-1422
    • (1976) J Biochem (Tokyo) , vol.80 , pp. 1411-1422
    • Nakamura, K.1    Mizushima, S.2
  • 11
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H., and Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49 (1985) 1-32
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 12
    • 0024592938 scopus 로고
    • Identification of porins in the outer membrane of Pseudomonas aeruginosa that form small diffusion pores
    • Yoshihara E., and Nakae T. Identification of porins in the outer membrane of Pseudomonas aeruginosa that form small diffusion pores. J Biol Chem 264 (1989) 6297-6301
    • (1989) J Biol Chem , vol.264 , pp. 6297-6301
    • Yoshihara, E.1    Nakae, T.2
  • 13
    • 0025968741 scopus 로고
    • Identification and characterization of porins in Pseudomonas aeruginosa
    • Nikaido H., Nikaido K., and Harayama S. Identification and characterization of porins in Pseudomonas aeruginosa. J Biol Chem 266 (1991) 770-779
    • (1991) J Biol Chem , vol.266 , pp. 770-779
    • Nikaido, H.1    Nikaido, K.2    Harayama, S.3
  • 14
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • Sugawara E., and Nikaido H. OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J Biol Chem 269 (1994) 17981-17987
    • (1994) J Biol Chem , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 15
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • Arora A., Rinehart D., Szabo G., and Tamm L. Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J Biol Chem 275 (2000) 1594-1600
    • (2000) J Biol Chem , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.4
  • 16
    • 0033816975 scopus 로고    scopus 로고
    • The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: correlation with a three-dimensional model
    • Brinkman F., Bains M., and Hancock R. The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: correlation with a three-dimensional model. J Bacteriol 182 (2000) 5251-5255
    • (2000) J Bacteriol , vol.182 , pp. 5251-5255
    • Brinkman, F.1    Bains, M.2    Hancock, R.3
  • 18
    • 0026713164 scopus 로고
    • The isolation and characterization of a major outer-membrane protein from Bacteroides distasonis
    • Wexler H., Getty C., and Fisher G. The isolation and characterization of a major outer-membrane protein from Bacteroides distasonis. J Med Microbiol 37 (1992) 165-175
    • (1992) J Med Microbiol , vol.37 , pp. 165-175
    • Wexler, H.1    Getty, C.2    Fisher, G.3
  • 19
    • 0036707372 scopus 로고    scopus 로고
    • Identification of an OmpA protein from Bacteroides fragilis: ompA gene sequence, OmpA amino acid sequence and predictions of protein structure
    • Wexler H., Read E., and Tomzynski T. Identification of an OmpA protein from Bacteroides fragilis: ompA gene sequence, OmpA amino acid sequence and predictions of protein structure. Anaerobe 8 (2002) 180-191
    • (2002) Anaerobe , vol.8 , pp. 180-191
    • Wexler, H.1    Read, E.2    Tomzynski, T.3
  • 20
    • 0036550867 scopus 로고    scopus 로고
    • Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis
    • Murakami Y., Imai M., Nakamura H., and Yoshimura F. Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis. Eur J Oral Sci 110 (2002) 157-162
    • (2002) Eur J Oral Sci , vol.110 , pp. 157-162
    • Murakami, Y.1    Imai, M.2    Nakamura, H.3    Yoshimura, F.4
  • 21
    • 0019824138 scopus 로고
    • Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli
    • Nikaido H., and Rosenberg E. Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J Gen Physiol 77 (1981) 121-135
    • (1981) J Gen Physiol , vol.77 , pp. 121-135
    • Nikaido, H.1    Rosenberg, E.2
  • 22
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins
    • Nikaido H., and Rosenberg E. Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. J Bacteriol 153 (1983) 241-252
    • (1983) J Bacteriol , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.2
  • 23
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157 (1982) 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 25
    • 0036855904 scopus 로고    scopus 로고
    • An evaluation of beta-turn prediction methods
    • Kaur H., and Raghava G. An evaluation of beta-turn prediction methods. Bioinformatics 18 (2002) 1508-1514
    • (2002) Bioinformatics , vol.18 , pp. 1508-1514
    • Kaur, H.1    Raghava, G.2
  • 26
    • 0037372098 scopus 로고    scopus 로고
    • Prediction of beta-turns in proteins from multiple alignment using neural network
    • Kaur H., and Raghava G. Prediction of beta-turns in proteins from multiple alignment using neural network. Protein Sci 12 (2003) 627-634
    • (2003) Protein Sci , vol.12 , pp. 627-634
    • Kaur, H.1    Raghava, G.2
  • 27
    • 8844252295 scopus 로고    scopus 로고
    • Prediction of β-turn types in proteins from evolutionary information using neural network
    • Kaur H., and Raghava G. Prediction of β-turn types in proteins from evolutionary information using neural network. Bioinformatics 20 (2004) 2751-2758
    • (2004) Bioinformatics , vol.20 , pp. 2751-2758
    • Kaur, H.1    Raghava, G.2
  • 28
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Int J Neural Syst 8 (1997) 581-599
    • (1997) Int J Neural Syst , vol.8 , pp. 581-599
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 29
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67 (2003) 593-656
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 30
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot R., and Vanderleyden J. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol Microbiol 12 (1994) 333-334
    • (1994) Mol Microbiol , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 31
    • 0028878069 scopus 로고
    • Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF
    • Rawling E., Martin N., and Hancock R. Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF. Infect Immun 63 (1995) 38-42
    • (1995) Infect Immun , vol.63 , pp. 38-42
    • Rawling, E.1    Martin, N.2    Hancock, R.3
  • 32
    • 0027449281 scopus 로고
    • Linker-insertion mutagenesis of Pseudomonas aeruginosa outer membrane protein OprF
    • Wong R., Jost H., and Hancock R. Linker-insertion mutagenesis of Pseudomonas aeruginosa outer membrane protein OprF. Mol Microbiol 10 (1993) 283-292
    • (1993) Mol Microbiol , vol.10 , pp. 283-292
    • Wong, R.1    Jost, H.2    Hancock, R.3
  • 33
    • 0029823940 scopus 로고    scopus 로고
    • Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
    • Sugawara E., Steiert M., Rouhani S., and Nikaido H. Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa. J Bacteriol 178 (1996) 6067-6069
    • (1996) J Bacteriol , vol.178 , pp. 6067-6069
    • Sugawara, E.1    Steiert, M.2    Rouhani, S.3    Nikaido, H.4
  • 34
    • 33745216927 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa porin OprF: properties of the channel
    • Nesterovich E., Sugavara E., Nikaido H., and Bezrukov S. Pseudomonas aeruginosa porin OprF: properties of the channel. J Biol Chem 281 (2006) 16230-16237
    • (2006) J Biol Chem , vol.281 , pp. 16230-16237
    • Nesterovich, E.1    Sugavara, E.2    Nikaido, H.3    Bezrukov, S.4
  • 35
    • 33745218065 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa porin OprF exists in two different conformations
    • Sugawara E., Nesterovich E., Bezrukov S., and Nikaido H. Pseudomonas aeruginosa porin OprF exists in two different conformations. J Biol Chem 281 (2006) 16220-16229
    • (2006) J Biol Chem , vol.281 , pp. 16220-16229
    • Sugawara, E.1    Nesterovich, E.2    Bezrukov, S.3    Nikaido, H.4
  • 36
    • 0022082599 scopus 로고
    • Folding patterns of porin and bacteriorhodopsin
    • Pautsch C., and Rosenbuch J. Folding patterns of porin and bacteriorhodopsin. EMBO J 4 (1985) 1593-1597
    • (1985) EMBO J , vol.4 , pp. 1593-1597
    • Pautsch, C.1    Rosenbuch, J.2
  • 37
    • 0027380391 scopus 로고
    • The major heat-modifiable outer membrane protein CD is highly conserved among strains of Branhamella catarrhalis
    • Murphy T., Kirkham C., and Lesse A. The major heat-modifiable outer membrane protein CD is highly conserved among strains of Branhamella catarrhalis. Mol Microbiol 10 (1993) 87-97
    • (1993) Mol Microbiol , vol.10 , pp. 87-97
    • Murphy, T.1    Kirkham, C.2    Lesse, A.3
  • 38
    • 0034695070 scopus 로고    scopus 로고
    • Involvement of the C-terminal part of Pseudomonas fluorescens OprF in the modulation of its pore-forming properties
    • El Hamel C., Freulet M., Jaquinod M., De E., Molle G., and Orange N. Involvement of the C-terminal part of Pseudomonas fluorescens OprF in the modulation of its pore-forming properties. Biochim Biophys Acta 1509 (2000) 237-244
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 237-244
    • El Hamel, C.1    Freulet, M.2    Jaquinod, M.3    De, E.4    Molle, G.5    Orange, N.6


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