메뉴 건너뛰기




Volumn 65, Issue 7, 2001, Pages 1617-1626

Azurin involved in alcohol oxidation system in Pseudomonas putida HK5: Expression analysis and gene cloning

Author keywords

Alcohol dehydrogenase; Azurin; PQQ; Pyrroloquinoline quinone; Quinoprotein

Indexed keywords

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS PUTIDA;

EID: 0035403353     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.1617     Document Type: Article
Times cited : (4)

References (34)
  • 3
    • 0028926926 scopus 로고
    • Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes
    • Edwards, S. L., Davidson, V. L., Hyun, Y.-L., and Wingfield, P. T., Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J. Biol., Chem., 270, 4293-4298 (1995).
    • (1995) J. Biol., Chem. , vol.270 , pp. 4293-4298
    • Edwards, S.L.1    Davidson, V.L.2    Hyun, Y.-L.3    Wingfield, P.T.4
  • 4
    • 0000270379 scopus 로고
    • Azurin from Pseudomonas putida: An acceptor for p-cresol methylhydroxylase
    • Causer, M. J., Hopper, D. J., McIntire, W. S., and Singer, T. P., Azurin from Pseudomonas putida: an acceptor for p-cresol methylhydroxylase. Biochem. Soc. Trans., 12, 1131-1132 (1984).
    • (1984) Biochem. Soc. Trans. , vol.12 , pp. 1131-1132
    • Causer, M.J.1    Hopper, D.J.2    McIntire, W.S.3    Singer, T.P.4
  • 6
    • 0029154216 scopus 로고
    • Cloning, sequencing and mutation of a gene for azurin in Methylobacillus flagellatum KT
    • Gak, E. R., Chistoserdov, A. Y., and Lidstrom, M. E., Cloning, sequencing and mutation of a gene for azurin in Methylobacillus flagellatum KT. J. Bacteriol., 177, 4575-4578 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 4575-4578
    • Gak, E.R.1    Chistoserdov, A.Y.2    Lidstrom, M.E.3
  • 7
    • 0029031697 scopus 로고
    • Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonasputida is grown on different alcohols
    • Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M., and Adachi, O., Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonasputida is grown on different alcohols. J Bacteriol., 177, 2442-2450 (1995).
    • (1995) J Bacteriol. , vol.177 , pp. 2442-2450
    • Toyama, H.1    Fujii, A.2    Matsushita, K.3    Shinagawa, E.4    Ameyama, M.5    Adachi, O.6
  • 8
    • 0033545967 scopus 로고    scopus 로고
    • Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5
    • Matsushita, K., Yamashita, T., Aoki, N., Toyama, H., and Adachi, O., Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry, 38, 6111-6118 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6111-6118
    • Matsushita, K.1    Yamashita, T.2    Aoki, N.3    Toyama, H.4    Adachi, O.5
  • 9
    • 0030771742 scopus 로고    scopus 로고
    • In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of RpoS and ANR
    • Vijgenboom, E., Busch, J. E., and Canters, G. W., In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of RpoS and ANR. Microbiology, 143, 2853-2863 (1997).
    • (1997) Microbiology , vol.143 , pp. 2853-2863
    • Vijgenboom, E.1    Busch, J.E.2    Canters, G.W.3
  • 10
    • 0023130391 scopus 로고
    • The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide
    • Canters, G. W., The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. FEBS Lett., 212, 167-172 (1987); Arvidsson, R. H. A., Nordling, M., and Lundberg, L. G., The azurin gene from Pseudomonas aeruginosa. Cloning and characterization. Eur. J. Biochem., 179, 195-200 (1989).
    • (1987) FEBS Lett. , vol.212 , pp. 167-172
    • Canters, G.W.1
  • 11
    • 0024517882 scopus 로고
    • The azurin gene from Pseudomonas aeruginosa. Cloning and characterization
    • Canters, G. W., The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. FEBS Lett., 212, 167-172 (1987); Arvidsson, R. H. A., Nordling, M., and Lundberg, L. G., The azurin gene from Pseudomonas aeruginosa. Cloning and characterization. Eur. J. Biochem., 179, 195-200 (1989).
    • (1989) Eur. J. Biochem. , vol.179 , pp. 195-200
    • Arvidsson, R.H.A.1    Nordling, M.2    Lundberg, L.G.3
  • 12
    • 0025311502 scopus 로고
    • Isolation and sequencing of the Alcaligenes denitrificans azurin encoding gene: Comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis
    • Hoitink, C. W. G., Woudt, L. P., Turenhout, J. C. M., van de Kamp, M., and Canters, G. W., Isolation and sequencing of the Alcaligenes denitrificans azurin encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis. Gene, 90, 15-20 (1990).
    • (1990) Gene , vol.90 , pp. 15-20
    • Hoitink, C.W.G.1    Woudt, L.P.2    Turenhout, J.C.M.3    Van De Kamp, M.4    Canters, G.W.5
  • 13
    • 0032059760 scopus 로고    scopus 로고
    • Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain
    • Taguchi, K., Kudo, T., and Tobari, J., Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain J. Biosci. Biotechnol. Biochem., 62, 870-874 (1998); Taguchi, K., Kudo, T., Tobari, J., Genetic organization and characterization of the mau gene cluster, which concerned the initial step of electron transport chains involved in methylamine oxidation of the obligate methylotroph Methylomonas sp. strain J. J. Ferment. Bioeng., 83, 502-510 (1997); Ambler, R. P., and Tobari, J, Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J. Biochem. J., 261, 495-499 (1989).
    • (1998) J. Biosci. Biotechnol. Biochem. , vol.62 , pp. 870-874
    • Taguchi, K.1    Kudo, T.2    Tobari, J.3
  • 14
    • 0031361823 scopus 로고    scopus 로고
    • Genetic organization and characterization of the mau gene cluster, which concerned the initial step of electron transport chains involved in methylamine oxidation of the obligate methylotroph Methylomonas sp. strain J
    • Taguchi, K., Kudo, T., and Tobari, J., Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain J. Biosci. Biotechnol. Biochem., 62, 870-874 (1998); Taguchi, K., Kudo, T., Tobari, J., Genetic organization and characterization of the mau gene cluster, which concerned the initial step of electron transport chains involved in methylamine oxidation of the obligate methylotroph Methylomonas sp. strain J. J. Ferment. Bioeng., 83, 502-510 (1997); Ambler, R. P., and Tobari, J, Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J. Biochem. J., 261, 495-499 (1989).
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 502-510
    • Taguchi, K.1    Kudo, T.2    Tobari, J.3
  • 15
    • 0024970798 scopus 로고
    • Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J
    • Taguchi, K., Kudo, T., and Tobari, J., Cloning and characterization of the azurin iso-1 gene, concerned with the electron transport chain involved in methylamine/methanol oxidation in the obligate methylotroph Methylomonas sp. strain J. Biosci. Biotechnol. Biochem., 62, 870-874 (1998); Taguchi, K., Kudo, T., Tobari, J., Genetic organization and characterization of the mau gene cluster, which concerned the initial step of electron transport chains involved in methylamine oxidation of the obligate methylotroph Methylomonas sp. strain J. J. Ferment. Bioeng., 83, 502-510 (1997); Ambler, R. P., and Tobari, J, Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J. Biochem. J., 261, 495-499 (1989).
    • (1989) Biochem. J. , vol.261 , pp. 495-499
    • Ambler, R.P.1    Tobari, J.2
  • 16
    • 0032031387 scopus 로고    scopus 로고
    • Crystallographic study of azurin from Pseudomonas putida
    • Chen, Z. W., Barber, M. J., McIntire, W. S., and Mathews, F. S., Crystallographic study of azurin from Pseudomonas putida. Acta Cryst., D54, 253-268 (1998).
    • (1998) Acta Cryst. , vol.D54 , pp. 253-268
    • Chen, Z.W.1    Barber, M.J.2    McIntire, W.S.3    Mathews, F.S.4
  • 17
    • 0029883559 scopus 로고    scopus 로고
    • Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans
    • Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E., and Adachi, O., Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem., 271, 4850-4857 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4850-4857
    • Matsushita, K.1    Yakushi, T.2    Toyama, H.3    Shinagawa, E.4    Adachi, O.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., Ryan, D., and Levin, W., An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem., 75, 168-176 (1976).
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 20
    • 0016642871 scopus 로고
    • A simple technique for estimation interference by detergents in the Lowry method of protein determination
    • Dulley, J. R., and Grieve, P. A., A simple technique for estimation interference by detergents in the Lowry method of protein determination. Anal. Biochem., 64, 136-141 (1975).
    • (1975) Anal. Biochem. , vol.64 , pp. 136-141
    • Dulley, J.R.1    Grieve, P.A.2
  • 21
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxynucleic acid from micro-organisms
    • Marmur, J., A procedure for the isolation of deoxynucleic acid from micro-organisms. J. Mol. Biol., 3, 208-218 (1961).
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 24
    • 0023512814 scopus 로고
    • The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells
    • Yamamoto, K., Uozumi, T., and Beppu, T., The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells. J. Bacteriol., 169, 5648-5652 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 5648-5652
    • Yamamoto, K.1    Uozumi, T.2    Beppu, T.3
  • 25
    • 0031051445 scopus 로고    scopus 로고
    • The pseudoazurin gene from Thiosphaera pantotropha: Analysis of upstream putative regulatory sequences and overexpression in Escherichia coli
    • Leimg, Y.-C., Chan, C., Reader, J. S., Willis, A. C., van Spanning, R. J. M., Ferguson, S. J., and Radford,S. E., The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and overexpression in Escherichia coli. Biochem. J., 321, 699-705 (1997).
    • (1997) Biochem. J. , vol.321 , pp. 699-705
    • Leimg, Y.-C.1    Chan, C.2    Reader, J.S.3    Willis, A.C.4    Van Spanning, R.J.M.5    Ferguson, S.J.6    Radford, S.E.7
  • 26
    • 0001425369 scopus 로고
    • A nitrite reducing system reconstructed with purified cytochrome components of Pseudomonas aeruginosa
    • Yamanaka, T., Ota, A., and Okunuki, K., A nitrite reducing system reconstructed with purified cytochrome components of Pseudomonas aeruginosa. Biochim. Biophys. Acta, 53, 294-308 (1961).
    • (1961) Biochim. Biophys. Acta , vol.53 , pp. 294-308
    • Yamanaka, T.1    Ota, A.2    Okunuki, K.3
  • 27
    • 0029670970 scopus 로고    scopus 로고
    • 54-dependent regulators: Derepression as a control mechanism
    • 54-dependent regulators: derepression as a control mechanism,. Mol. Microbiol., 19, 409-416 (1996).
    • (1996) Mol. Microbiol. , vol.19 , pp. 409-416
    • Shingler, V.1
  • 29
    • 0032724622 scopus 로고    scopus 로고
    • Mechanisms for redox control of gene expression
    • Bauer, C. E., Elsen, S., and Bird, T. H., Mechanisms for redox control of gene expression. Ann. Rev. Microbiol., 53, 495-523 (1999).
    • (1999) Ann. Rev. Microbiol. , vol.53 , pp. 495-523
    • Bauer, C.E.1    Elsen, S.2    Bird, T.H.3
  • 30
    • 0025129999 scopus 로고
    • Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH and the fnr gene product
    • Cotter, P. A., Chepuri, V., Gennis, R. B., and Gunsalus, R. P., Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH and the fnr gene product. J. Bacteriol., 172, 6333-6338 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 6333-6338
    • Cotter, P.A.1    Chepuri, V.2    Gennis, R.B.3    Gunsalus, R.P.4
  • 31
    • 0024314879 scopus 로고
    • FNR-dependent repression of ndh gene of Escherichia coli and metal requirement for FNR-regulated gene expression
    • Spiro, S., Roberts, R. E., and Guest, J. R., FNR-dependent repression of ndh gene of Escherichia coli and metal requirement for FNR-regulated gene expression. Mol. Microbiol., 3, 601-608 (1989).
    • (1989) Mol. Microbiol. , vol.3 , pp. 601-608
    • Spiro, S.1    Roberts, R.E.2    Guest, J.R.3
  • 32
    • 0029863879 scopus 로고    scopus 로고
    • The homologous regulators ANR of Pseudomonas aeruginosa and FNR of Escherichia coli have overlapping but distinct specificities for anaerobically inducible promoters
    • Winteler H. V., and Haas, D., The homologous regulators ANR of Pseudomonas aeruginosa and FNR of Escherichia coli have overlapping but distinct specificities for anaerobically inducible promoters. Microbiology, 142, 685-693 (1996).
    • (1996) Microbiology , vol.142 , pp. 685-693
    • Winteler, H.V.1    Haas, D.2
  • 33
    • 0033229925 scopus 로고    scopus 로고
    • Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): A soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS)
    • Chen, Z. W., Baruch, P., Mathews, F. S., Matsushita, K., Yamashita, T., Toyama, H., and Adachi, O., Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS). Acta Crystallogr. D Biol. Crystallogr., 55, 1933-1936 (1999).
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1933-1936
    • Chen, Z.W.1    Baruch, P.2    Mathews, F.S.3    Matsushita, K.4    Yamashita, T.5    Toyama, H.6    Adachi, O.7
  • 34
    • 0009879715 scopus 로고    scopus 로고
    • Electron transport systems for quinohemoprotein type II alcohol dehydrogenase of Pseudomonas putida HK5
    • eds. Iriarte, A., Kagan, H. M., and Martinez-Carrion, M., Birkhauser, Basel-Boston-Berlin
    • 6 and PQQ-dependent proteins", eds. Iriarte, A., Kagan, H. M., and Martinez-Carrion, M., Birkhauser, Basel-Boston-Berlin, pp. 219-224 (2000).
    • (2000) 6 and PQQ-dependent Proteins , pp. 219-224
    • Matsushita, K.1    Yamashita, T.2    Aoki, N.3    Toyama, H.4    Adachi, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.