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Volumn 173, Issue 5-6, 2000, Pages 346-351

Molecular analysis of an outer membrane protein, MopB, of Methylococcus capsulatus (Bath) and structural comparisons with proteins of the OmpA family

Author keywords

Methanotroph; Methylococcus capsulatus; OmpA protein; OprF protein; Outer membrane protein

Indexed keywords

BACTERIAL PROTEIN; MOPB PROTEIN; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; UNCLASSIFIED DRUG;

EID: 0034047830     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030000151     Document Type: Article
Times cited : (9)

References (36)
  • 2
    • 0027374969 scopus 로고
    • Revised taxonomy of the methanotrophs: Description of Methylobacter gen. Nov., emendation of Methylococcus, validation of Methylosinus and Methylocystis species, and a proposal that the family Methylococcaceae includes only the group I methanotrophs
    • Bowman JP, Sly LI, Nichols PD, Hayward AC (1993) Revised taxonomy of the methanotrophs: description of Methylobacter gen. nov., emendation of Methylococcus, validation of Methylosinus and Methylocystis species, and a proposal that the family Methylococcaceae includes only the group I methanotrophs. Int J Syst Bacteriol 43:735-753
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 735-753
    • Bowman, J.P.1    Sly, L.I.2    Nichols, P.D.3    Hayward, A.C.4
  • 3
    • 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, Vanderleyden J (1994a) 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 [letter]. Mol Microbiol 12:333-334
    • (1994) Mol Microbiol , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 4
    • 0028284209 scopus 로고
    • A conserved surface-exposed domain in major outer membrane proteins of pathogenic Pseudomonas and Branhamella species shares sequence homology with the calcium-binding repeats of the eukaryotic extracellular matrix protein throbospondin
    • De Mot R, Vanderleyden J (1994b) A conserved surface-exposed domain in major outer membrane proteins of pathogenic Pseudomonas and Branhamella species shares sequence homology with the calcium-binding repeats of the eukaryotic extracellular matrix protein throbospondin. Mol Microbiol 13: 379-380
    • (1994) Mol Microbiol , vol.13 , pp. 379-380
    • De Mot, R.1    Vanderleyden, J.2
  • 7
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou G, Stathopoulos C, Daugherty PS, Nayak AR, Iverson BL, Curtiss R III (1997) Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol 15:29-34
    • (1997) Nat Biotechnol , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss R. III6
  • 9
    • 0028006525 scopus 로고
    • Identification and characterization of the Treponema pallidum tpn50 gene, an ompA homolog
    • Hardham JM, Stamm LV (1994) Identification and characterization of the Treponema pallidum tpn50 gene, an ompA homolog. Infect Immun 62:1015-1025
    • (1994) Infect Immun , vol.62 , pp. 1015-1025
    • Hardham, J.M.1    Stamm, L.V.2
  • 10
    • 0026661091 scopus 로고
    • Presence of methyl sterol and bacteriohopanpolyol in an outer-membrane preparation from Methylococcus capsulatus (Bath)
    • Jahnke LL, Stan-Lotter H, Kato K, Hochstein LI (1992) Presence of methyl sterol and bacteriohopanpolyol in an outer-membrane preparation from Methylococcus capsulatus (Bath). J Gen Microbiol 138:1759-1766
    • (1992) J Gen Microbiol , vol.138 , pp. 1759-1766
    • Jahnke, L.L.1    Stan-Lotter, H.2    Kato, K.3    Hochstein, L.I.4
  • 11
    • 0003607510 scopus 로고
    • The porin superfamily: Diversity and common features
    • Ghuysen J-M, Hakenbeck R (eds) Elsevier, Amsterdam
    • Janteur D, Lakey JH, Pattus F (1994) The porin superfamily: diversity and common features. In: Ghuysen J-M, Hakenbeck R (eds) Bacterial cell wall. Elsevier, Amsterdam, pp 363-380
    • (1994) Bacterial Cell Wall , pp. 363-380
    • Janteur, D.1    Lakey, J.H.2    Pattus, F.3
  • 12
    • 0029975020 scopus 로고    scopus 로고
    • Reduction of RNA and DNA in Methylococcus capsulatus by endogenous nucleases
    • Larsen J, Joergensen L (1996) Reduction of RNA and DNA in Methylococcus capsulatus by endogenous nucleases. Appl Microbiol Biotechnol 45:137-140
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 137-140
    • Larsen, J.1    Joergensen, L.2
  • 13
    • 0025168744 scopus 로고
    • Methylotrophs: Genetics and commercial applications
    • Lidstrom ME, Stirling DI (1990) Methylotrophs: genetics and commercial applications. Annu Rev Microbiol 44:27-58
    • (1990) Annu Rev Microbiol , vol.44 , pp. 27-58
    • Lidstrom, M.E.1    Stirling, D.I.2
  • 14
    • 0023829903 scopus 로고
    • 'DNA strider': A 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers
    • Marck C (1988) 'DNA Strider': a 'C' program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucleic Acids Res 16:1829-1836
    • (1988) Nucleic Acids Res , vol.16 , pp. 1829-1836
    • Marck, C.1
  • 15
    • 0021213980 scopus 로고
    • Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: Analysis of mutant genes expressing altered proteins
    • Morona R, Klose M, Henning U (1984) Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins. J Bacteriol 159:570-578
    • (1984) J Bacteriol , vol.159 , pp. 570-578
    • Morona, R.1    Klose, M.2    Henning, U.3
  • 16
    • 0027380391 scopus 로고
    • The major heat-modifiable outer membrane protein CD is highly conserved among strains of Branhamella catarrhalis
    • Murphy TF, Kirkham C, Lesse AJ (1993) The major heat-modifiable outer membrane protein CD is highly conserved among strains of Branhamella catarrhalis. Mol Microbiol 10:87-97
    • (1993) Mol Microbiol , vol.10 , pp. 87-97
    • Murphy, T.F.1    Kirkham, C.2    Lesse, A.J.3
  • 17
    • 0032794698 scopus 로고    scopus 로고
    • Analysis of antigenic structure and human immune response to outer membrane protein CD of Moraxellalla catarrhalis
    • Murphy TF, Kirkham C, DeNardin E, Sethi S (1999) Analysis of antigenic structure and human immune response to outer membrane protein CD of Moraxellalla catarrhalis. Mol Microbiol 67:4578-4585
    • (1999) Mol Microbiol , vol.67 , pp. 4578-4585
    • Murphy, T.F.1    Kirkham, C.2    Denardin, E.3    Sethi, S.4
  • 18
    • 0002708140 scopus 로고
    • The genetics and molecular biology of obligate methane-oxidizing bacteria
    • Murrell JC, Dalton H (eds) Plenum, New York
    • Murrell JC (1992) The genetics and molecular biology of obligate methane-oxidizing bacteria. In: Murrell JC, Dalton H (eds) Methane and methanol utilizers. Plenum, New York, pp 115-148
    • (1992) Methane and Methanol Utilizers , pp. 115-148
    • Murrell, J.C.1
  • 19
    • 0002017726 scopus 로고
    • nifH genes in the obligate methane oxidizing bacteria
    • Oakley CJ, Murrell JC (1988) nifH genes in the obligate methane oxidizing bacteria. FEMS Microbiol Lett 49:53-57
    • (1988) FEMS Microbiol Lett , vol.49 , pp. 53-57
    • Oakley, C.J.1    Murrell, J.C.2
  • 20
    • 0028143645 scopus 로고
    • Quantitative electrophoretic analysis of proteins labeled with monobromobimane
    • O'Keefe DO (1994) Quantitative electrophoretic analysis of proteins labeled with monobromobimane. Anal Biochem 222: 86-94
    • (1994) Anal Biochem , vol.222 , pp. 86-94
    • O'Keefe, D.O.1
  • 21
    • 0023515798 scopus 로고
    • Prokaryotic hopanoids and other polyterpenoid sterol surrogates
    • Ourisson G, Rohmer M, Poralla K (1987) Prokaryotic hopanoids and other polyterpenoid sterol surrogates. Annu Rev Microbiol 41:301-333
    • (1987) Annu Rev Microbiol , vol.41 , pp. 301-333
    • Ourisson, G.1    Rohmer, M.2    Poralla, K.3
  • 22
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A, Schultz GE (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5:1013-1017
    • (1998) Nat Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schultz, G.E.2
  • 23
    • 0028878069 scopus 로고
    • Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF
    • Rawling EG, Martin NL, Hancock REW (1995) Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF. Infect Immun 63:38-42
    • (1995) Infect Immun , vol.63 , pp. 38-42
    • Rawling, E.G.1    Martin, N.L.2    Hancock, R.E.W.3
  • 24
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins RD, Kaneva I, Mulchandani A, Chen W (1997) Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nat Biotechnol 15:984-987
    • (1997) Nat Biotechnol , vol.15 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 25
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • Rost B, Sander C (1993) Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc Natl Acad Sci USA 90:7558-7562
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 27
    • 0025025399 scopus 로고
    • Rapid isolation of miniprep DNA for double strand sequencing
    • Saunders SE, Burke JF (1990) Rapid isolation of miniprep DNA for double strand sequencing. Nucleic Acids Res 18:4948
    • (1990) Nucleic Acids Res , vol.18 , pp. 4948
    • Saunders, S.E.1    Burke, J.F.2
  • 29
    • 0018150270 scopus 로고
    • Cell envelope and cell shape of Escherichia coli: Multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag I, Schwartz H, Hirota Y, Hennig U (1978) Cell envelope and cell shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol 136:280-285
    • (1978) J Bacteriol , vol.136 , pp. 280-285
    • Sonntag, I.1    Schwartz, H.2    Hirota, Y.3    Hennig, U.4
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 0026057350 scopus 로고
    • Conservation of the gene for outer membrane protein OprF in the family Pseudomonadaceae: Sequence of the Pseudomonas syringae oprF gene
    • Ullstrom CA, Siehnel R, Woodruff W, Steinbach S, Hancock REW (1991) Conservation of the gene for outer membrane protein OprF in the family Pseudomonadaceae: sequence of the Pseudomonas syringae oprF gene. J Bacteriol 173:768-775
    • (1991) J Bacteriol , vol.173 , pp. 768-775
    • Ullstrom, C.A.1    Siehnel, R.2    Woodruff, W.3    Steinbach, S.4    Hancock, R.E.W.5
  • 32
    • 0032179733 scopus 로고    scopus 로고
    • Bioaccumulation of heavy metals with protein fusions of metallothionein to bacterial OMPs
    • Valls A, Gonzáles-Duarte R, Atrian S, De Lorenzo V (1998) Bioaccumulation of heavy metals with protein fusions of metallothionein to bacterial OMPs. Biochimie 80:855-861
    • (1998) Biochimie , vol.80 , pp. 855-861
    • Valls, A.1    Gonzáles-Duarte, R.2    Atrian, S.3    Lorenzo D. V4
  • 34
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • Von Heijne G (1985) Signal sequences. The limits of variation. J Mol Biol 184:99-105
    • (1985) J Mol Biol , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 35
    • 0000574005 scopus 로고
    • Methylococcaceae
    • Krieg NR, Holt JG (eds) Williams and Wilkins, Baltimore
    • Whittenbury R, Krieg NR (1984) Methylococcaceae. In: Krieg NR, Holt JG (eds) Bergey's manual of systematic bacteriology, vol 1. Williams and Wilkins, Baltimore, pp 256-261
    • (1984) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 256-261
    • Whittenbury, R.1    Krieg, N.R.2
  • 36
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli OmpA protein
    • Woodruff WA, Hancock REW (1989) Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J Bacteriol 171:3304-3309
    • (1989) J Bacteriol , vol.171 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.