메뉴 건너뛰기




Volumn 85, Issue 5, 1998, Pages 875-882

Identification of a gene for a rubrerythrin/nigerythrin-like protein in Spirillum volutans by using amino acid sequence data from mass spectrometry and NH2-terminal sequencing

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CLONING; CLOSTRIDIUM; GENES; MASS SPECTROMETRY;

EID: 0031795970     PISSN: 13645072     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2672.1998.00602.x     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 0029767454 scopus 로고    scopus 로고
    • Improved method for colony counts of the microaerophile Spirillum volutans
    • Alban, P.S. and Krieg, N.R. (1996) Improved method for colony counts of the microaerophile Spirillum volutans. Canadian Journal of Microbiology 42, 701-704.
    • (1996) Canadian Journal of Microbiology , vol.42 , pp. 701-704
    • Alban, P.S.1    Krieg, N.R.2
  • 2
    • 0031982010 scopus 로고    scopus 로고
    • A hydrogen peroxide-resistant mutant of Spirillum volutans has NADH peroxidase activity but no increased oxygen tolerance
    • Alban, P.S. and Krieg, N.R. (1998) A hydrogen peroxide-resistant mutant of Spirillum volutans has NADH peroxidase activity but no increased oxygen tolerance. Canadian Journal of Microbiology 44, 87-91.
    • (1998) Canadian Journal of Microbiology , vol.44 , pp. 87-91
    • Alban, P.S.1    Krieg, N.R.2
  • 4
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C. and Fridovich, I. (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Analytical Biochemistry 44, 276-287.
    • (1971) Analytical Biochemistry , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 16044367245 scopus 로고    scopus 로고
    • The genome of Methanoccoccus jannaschii
    • Bult, C.J., White, O., Olsen, G.J. et al. (1996) The genome of Methanoccoccus jannaschii. Science 273, 1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3
  • 8
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman, M.F., Morgan, R.W., Jacobson, F.S. and Ames, B.N. (1985) Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41, 753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 9
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins
    • Christman, M.F., Storz, G. and Ames, B.N. (1989) OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proceedings of the National Academy of Sciences USA 86, 3484-3488.
    • (1989) Proceedings of the National Academy of Sciences USA , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 10
    • 0025847092 scopus 로고
    • Regulation of the oxidative stress response by the hpr gene in Bacillus subtilis
    • Dowds, B.C.A. and Hoch, J.A. (1991) Regulation of the oxidative stress response by the hpr gene in Bacillus subtilis. Journal of General Microbiology 137, 1121-1125.
    • (1991) Journal of General Microbiology , vol.137 , pp. 1121-1125
    • Dowds, B.C.A.1    Hoch, J.A.2
  • 11
    • 0023192484 scopus 로고
    • Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide
    • Imlay, J.A. and Linn, S. (1987) Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide. Journal of Bacteriology 169, 2967-2976.
    • (1987) Journal of Bacteriology , vol.169 , pp. 2967-2976
    • Imlay, J.A.1    Linn, S.2
  • 12
    • 0030961164 scopus 로고    scopus 로고
    • Oxygen-dependent growth of the obligate anaerobe Desulfovibrio vulgaris Hildenborough
    • Johnson, M.S., Zhulin, I.B., Gapuzan, M.K. and Taylor, B.L. (1997) Oxygen-dependent growth of the obligate anaerobe Desulfovibrio vulgaris Hildenborough. Journal of Bacteriology 179, 5598-5601.
    • (1997) Journal of Bacteriology , vol.179 , pp. 5598-5601
    • Johnson, M.S.1    Zhulin, I.B.2    Gapuzan, M.K.3    Taylor, B.L.4
  • 13
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archeoglobus fulgidus
    • Klenk, H.-P., Clayton, R.A., Tomb, J.-F. et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archeoglobus fulgidus. Nature 390, 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.-P.1    Clayton, R.A.2    Tomb, J.-F.3
  • 14
    • 0026318136 scopus 로고
    • Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris: Identification of potential ligands to the diiron site
    • Kurtz, D.M. and Prickril, B. (1991) Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris: identification of potential ligands to the diiron site. Biochemical and Biophysical Research Communications 181, 337-341.
    • (1991) Biochemical and Biophysical Research Communications , vol.181 , pp. 337-341
    • Kurtz, D.M.1    Prickril, B.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0030474295 scopus 로고    scopus 로고
    • Rubrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function
    • Lehmann, Y., Meile, L. and Teuber, M. (1996) Rubrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. Journal of Bacteriology 178, 7152-7158.
    • (1996) Journal of Bacteriology , vol.178 , pp. 7152-7158
    • Lehmann, Y.1    Meile, L.2    Teuber, M.3
  • 18
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. (1961) A procedure for the isolation of deoxyribonucleic acid from microorganisms. Journal of Molecular Biology 3, 208-218.
    • (1961) Journal of Molecular Biology , vol.3 , pp. 208-218
    • Marmur, J.1
  • 19
    • 0023357783 scopus 로고
    • Negative and positive assays of superoxide dismutase based on hematoxylin autooxidation
    • Martin, J.P. Jr, Dailey, M. and Sugarman, E. (1987) Negative and positive assays of superoxide dismutase based on hematoxylin autooxidation. Archives of Biochemistry and Biophysics 255, 329-3336.
    • (1987) Archives of Biochemistry and Biophysics , vol.255 , pp. 329-3336
    • Martin Jr., J.P.1    Dailey, M.2    Sugarman, E.3
  • 22
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • Norlund, P. and Eklund, H. (1993) Structure and function of the Escherichia coli ribonucleotide reductase protein R2. Journal of Molecular Biology 231, 123-164.
    • (1993) Journal of Molecular Biology , vol.231 , pp. 123-164
    • Norlund, P.1    Eklund, H.2
  • 23
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. Journal of Biological Chemistry 250, 4007-4021.
    • (1975) Journal of Biological Chemistry , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 24
    • 85153310884 scopus 로고
    • The microaerophile Spirillum volutans: Cultivation on complex liquid and solid media
    • Padgett, P.J., Cover, W.H. and Krieg, N.R. (1982) The microaerophile Spirillum volutans: cultivation on complex liquid and solid media. Canadian Journal of Microbiology 43, 466-477.
    • (1982) Canadian Journal of Microbiology , vol.43 , pp. 466-477
    • Padgett, P.J.1    Cover, W.H.2    Krieg, N.R.3
  • 25
    • 0022481735 scopus 로고
    • Factors relating to the aerotolerance of Spirillum volutans
    • Padgett, P.J. and Krieg, N.R. (1986) Factors relating to the aerotolerance of Spirillum volutans. Canadian Journal of Microbiology 32, 548-552.
    • (1986) Canadian Journal of Microbiology , vol.32 , pp. 548-552
    • Padgett, P.J.1    Krieg, N.R.2
  • 26
    • 0026347046 scopus 로고
    • Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenborough)
    • Prickril, B.C., Kurtz, D.N. Jr and Legall, J. (1991) Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenborough). Biochemistry 30, 11118-11123.
    • (1991) Biochemistry , vol.30 , pp. 11118-11123
    • Prickril, B.C.1    Kurtz Jr., D.N.2    Legall, J.3
  • 27
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig, A., Frederick, C.A., Lippard, S.J. and Norlund, P. (1993) Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 366, 537-543.
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.1    Frederick, C.A.2    Lippard, S.J.3    Norlund, P.4
  • 28
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Analytical Chemistry 68, 850-858.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 29
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum H: Functional analysis and comparative genomics
    • Smith, D.R., Doucette-Stamm, L.A., Deloughery, C. et al. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum H: functional analysis and comparative genomics. Journal of Bacteriology 179, 7135-7155.
    • (1997) Journal of Bacteriology , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3
  • 30
    • 0019882018 scopus 로고
    • Silver staining of proteins on polyacrylamide gel
    • Wray, W., Boulikas, T. and Wray, V.P. (1981) Silver staining of proteins on polyacrylamide gel. Analytical Biochemistry 118, 197-203.
    • (1981) Analytical Biochemistry , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3
  • 31
    • 0030739282 scopus 로고    scopus 로고
    • DNA similarity analysis of a putative ancient isolate obtained from amber
    • Yousten, A.A. and Rippere, K.E. (1997) DNA similarity analysis of a putative ancient isolate obtained from amber. FEMS Microbiology Letters 152, 345-347.
    • (1997) FEMS Microbiology Letters , vol.152 , pp. 345-347
    • Yousten, A.A.1    Rippere, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.