메뉴 건너뛰기




Volumn 178, Issue 13, 1996, Pages 3899-3907

Disruption of the serine proteinase gene (sep) in Aspergillus flavus leads to a compensatory increase in the expression of a metalloproteinase gene (mep20)

Author keywords

[No Author keywords available]

Indexed keywords

DYFLOS; HYGROMYCIN; MESSENGER RNA; METALLOPROTEINASE; SERINE PROTEINASE; SUBTILISIN; TRITIUM;

EID: 0029889602     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.13.3899-3907.1996     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 0025824448 scopus 로고
    • Identification of fungal cutinase promoter that is inducible by a plant signal via a phosphorylated trans-acting factor
    • Bajar, A., G. K. Podila, and P. E. Kolattukudy. 1991. Identification of fungal cutinase promoter that is inducible by a plant signal via a phosphorylated trans-acting factor. Proc. Natl. Acad. Sci. USA 88:8208-8212.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8208-8212
    • Bajar, A.1    Podila, G.K.2    Kolattukudy, P.E.3
  • 2
    • 0025196089 scopus 로고
    • 2+-dependent functions in Yersinia pestis
    • 2+-dependent functions in Yersinia pestis. J. Bacteriol. 172:4661-4671.
    • (1990) J. Bacteriol. , vol.172 , pp. 4661-4671
    • Barve, S.S.1    Straley, S.C.2
  • 3
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheria
    • Boyd, J., M. N. Oza, and J. R. Murphy. 1990. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheria. Proc. Natl. Acad. Sci. USA 87:5968-5972.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 4
    • 0019551730 scopus 로고
    • Western blotting: Electrophoretic transfer of proteins from SDS-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. H. 1981. Western blotting: electrophoretic transfer of proteins from SDS-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112: 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.H.1
  • 5
    • 0000575462 scopus 로고
    • Clinical manifestations and management of aspergillosis in the compromised patient
    • D. W. Warnock and M. D. Richardson (ed.), John Wiley and Sons, New York
    • Cohen, J. 1991. Clinical manifestations and management of aspergillosis in the compromised patient, p. 118-152. In D. W. Warnock and M. D. Richardson (ed.), Fungal infection in the compromised patient. John Wiley and Sons, New York.
    • (1991) Fungal Infection in the Compromised Patient , pp. 118-152
    • Cohen, J.1
  • 7
    • 0024382180 scopus 로고
    • Common themes in microbial pathogenicity
    • Finlay, B. B., and S. Falkow. 1989. Common themes in microbial pathogenicity. Microbiol. Rev. 53:210-230.
    • (1989) Microbiol. Rev. , vol.53 , pp. 210-230
    • Finlay, B.B.1    Falkow, S.2
  • 9
    • 0027140429 scopus 로고
    • Bacterial extracellular zinc-containing metalloproteinases
    • Hase, C. C., and R. A. Finkelstein. 1993. Bacterial extracellular zinc-containing metalloproteinases. Microbiol. Rev. 57:823-837.
    • (1993) Microbiol. Rev. , vol.57 , pp. 823-837
    • Hase, C.C.1    Finkelstein, R.A.2
  • 10
    • 0025782729 scopus 로고
    • Raw soy and purified proteinase inhibitors induce the appearance of inhibitor-resistant trypsin and chymotrypsin activities in Wistar rat duodenal juice
    • Holm, H., A. Jorgensen, and L. E. Hanssen. 1991. Raw soy and purified proteinase inhibitors induce the appearance of inhibitor-resistant trypsin and chymotrypsin activities in Wistar rat duodenal juice. J. Nutr. 121:532-538.
    • (1991) J. Nutr. , vol.121 , pp. 532-538
    • Holm, H.1    Jorgensen, A.2    Hanssen, L.E.3
  • 11
    • 0023909419 scopus 로고
    • High and low inhibitor soybean meals affect human duodenal proteinase activity differently: In vitro comparison of proteinase inhibition
    • Holm, H., A. Krogdahl, and L. E. Hanssen. 1988. High and low inhibitor soybean meals affect human duodenal proteinase activity differently: in vitro comparison of proteinase inhibition. J. Nutr. 118:521-525.
    • (1988) J. Nutr. , vol.118 , pp. 521-525
    • Holm, H.1    Krogdahl, A.2    Hanssen, L.E.3
  • 12
    • 0027940569 scopus 로고
    • Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans
    • Hube, B., M. Monod, D. A. Schofield, A. J. P. Brown, and N. A. R. Gow. 1994. Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans. Mol. Microbiol. 14:87-99.
    • (1994) Mol. Microbiol. , vol.14 , pp. 87-99
    • Hube, B.1    Monod, M.2    Schofield, D.A.3    Brown, A.J.P.4    Gow, N.A.R.5
  • 13
    • 0024234788 scopus 로고
    • Pancreatic enzyme secretion mediated by novel peptide: Monitor peptide hypothesis
    • Iwai, K., T. Fushiki, and S. Fukuoka. 1988. Pancreatic enzyme secretion mediated by novel peptide: monitor peptide hypothesis. Pancreas 3:720-728.
    • (1988) Pancreas , vol.3 , pp. 720-728
    • Iwai, K.1    Fushiki, T.2    Fukuoka, S.3
  • 15
    • 0027119999 scopus 로고
    • Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus
    • Jaton-Ogay, K., M. Suter, R. Crameri, R. Falchetto, A. Faith, and M. Monod. 1992. Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus. FEMS Microbiol. Lett. 92:162-168.
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 162-168
    • Jaton-Ogay, K.1    Suter, M.2    Crameri, R.3    Falchetto, R.4    Faith, A.5    Monod, M.6
  • 16
    • 0029128219 scopus 로고
    • Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition
    • Jongsma, M. A., P. L. Bakker, J. Peters, D. Bosch, and W. J. Stiekema. 1995. Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition. Proc. Natl. Acad. Sci. USA 92:8041-8045.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8041-8045
    • Jongsma, M.A.1    Bakker, P.L.2    Peters, J.3    Bosch, D.4    Stiekema, W.J.5
  • 17
    • 0028568211 scopus 로고
    • Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease
    • Katz, M. E., R. N. Rice, and B. F. Cheetham. 1994. Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease. Gene 150:287-292.
    • (1994) Gene , vol.150 , pp. 287-292
    • Katz, M.E.1    Rice, R.N.2    Cheetham, B.F.3
  • 18
    • 0027258413 scopus 로고
    • Erwinia chrysanthemi EC16 produces a second set of plant-inducible pectate lyase isozymes
    • Kelemu, S., and A. Collmer. 1993. Erwinia chrysanthemi EC16 produces a second set of plant-inducible pectate lyase isozymes. Appl. Environ. Microbiol. 59:1756-1761.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1756-1761
    • Kelemu, S.1    Collmer, A.2
  • 20
    • 0021349201 scopus 로고
    • Correlation of elastase production by some strains of Aspergillus fumigatus with ability to cause pulmonary invasive aspergillosis in mice
    • Kothary, M. H., T. Chase, Jr., and J. D. Macmillan. 1984. Correlation of elastase production by some strains of Aspergillus fumigatus with ability to cause pulmonary invasive aspergillosis in mice. Infect. Immun. 43:320-325.
    • (1984) Infect. Immun. , vol.43 , pp. 320-325
    • Kothary, M.H.1    Chase Jr., T.2    Macmillan, J.D.3
  • 21
    • 0021796963 scopus 로고
    • Genetic evidence for role of extracellular proteinase in virulence of Candida albicans
    • Kwon-Chung, K. J., D. Lehman, C. Good, and P. T. Magee. 1985. Genetic evidence for role of extracellular proteinase in virulence of Candida albicans. Infect. Immun. 49:571-575.
    • (1985) Infect. Immun. , vol.49 , pp. 571-575
    • Kwon-Chung, K.J.1    Lehman, D.2    Good, C.3    Magee, P.T.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029125381 scopus 로고
    • Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lungs
    • Lee, J. D., and P. E. Kolattukudy. 1995. Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lungs. Infect. Immun. 63:3796-3803.
    • (1995) Infect. Immun. , vol.63 , pp. 3796-3803
    • Lee, J.D.1    Kolattukudy, P.E.2
  • 24
    • 0029670357 scopus 로고    scopus 로고
    • Inhibition of Aspergillus serine proteinase by Streptomyces subtilisin inhibitor and high-level expression of this inhibitor in Pichia pastoris
    • Markaryan, A., C. J. Beall, and P. E. Kolattukudy. 1996. Inhibition of Aspergillus serine proteinase by Streptomyces subtilisin inhibitor and high-level expression of this inhibitor in Pichia pastoris. Biochem. Biophys. Res. Commun. 220:372-376.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 372-376
    • Markaryan, A.1    Beall, C.J.2    Kolattukudy, P.E.3
  • 26
    • 0028340071 scopus 로고
    • Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung
    • Markaryan, A., I. Morozova, H. Yu, and P. E. Kolattukudy. 1994. Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung. Infect. Immun. 62:2149-2157.
    • (1994) Infect. Immun. , vol.62 , pp. 2149-2157
    • Markaryan, A.1    Morozova, I.2    Yu, H.3    Kolattukudy, P.E.4
  • 27
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • Mekalanos, J. J. 1992. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 174:1-7.
    • (1992) J. Bacteriol. , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 28
    • 0017567709 scopus 로고
    • Relationship between the proteolytic activity of Aspergillus fumigatus and the fungus's invasiveness of mouse brain
    • Miyaji, M., and K. Nishimura. 1977. Relationship between the proteolytic activity of Aspergillus fumigatus and the fungus's invasiveness of mouse brain. Mycopathologia 62:161-166.
    • (1977) Mycopathologia , vol.62 , pp. 161-166
    • Miyaji, M.1    Nishimura, K.2
  • 29
    • 0027377215 scopus 로고
    • Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus
    • Monod, M., S. Paris, D. Sanglard, K. Jaton-Ogay, J. Billie, and J. P. Latgé. 1993. Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus. Infect. Immun. 61:4099-4104.
    • (1993) Infect. Immun. , vol.61 , pp. 4099-4104
    • Monod, M.1    Paris, S.2    Sanglard, D.3    Jaton-Ogay, K.4    Billie, J.5    Latgé, J.P.6
  • 31
    • 0002238821 scopus 로고
    • Pseudomonas metalloproteases and the host-microbe relationship
    • R. B. Fick, (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Parmley, M. J. 1993. Pseudomonas metalloproteases and the host-microbe relationship, p. 79-94. In R. B. Fick, (ed.), Pseudomonas aeruginosa the opportunist: pathogcnesis and disease. CRC Press, Inc., Boca Raton, Fla.
    • (1993) Pseudomonas Aeruginosa the Opportunist: Pathogcnesis and Disease , pp. 79-94
    • Parmley, M.J.1
  • 33
    • 0026517228 scopus 로고
    • Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755)
    • Poulet, S., D. Hauser, M. Quanz, H. Niemann, and M. R. Popoff. 1992. Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755). Biochem. Biophys. Res. Commun. 183:107-113.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 107-113
    • Poulet, S.1    Hauser, D.2    Quanz, M.3    Niemann, H.4    Popoff, M.R.5
  • 34
    • 0028144296 scopus 로고
    • Isolation, characterization, and cloning of the cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus
    • Ramesh, M. V., T. Sirakova, and P. E. Kolattukudy. 1994 Isolation, characterization, and cloning of the cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus. Infect. Immun. 62:79-85.
    • (1994) Infect. Immun. , vol.62 , pp. 79-85
    • Ramesh, M.V.1    Sirakova, T.2    Kolattukudy, P.E.3
  • 35
    • 0028837587 scopus 로고
    • Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteinases from Aspergillus flavus and A fumigatus
    • Ramesh, M. V., T. Sirakova, and P. E. Kolattukudy. 1995. Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteinases from Aspergillus flavus and A fumigatus. Gene 165:121-125.
    • (1995) Gene , vol.165 , pp. 121-125
    • Ramesh, M.V.1    Sirakova, T.2    Kolattukudy, P.E.3
  • 36
    • 0025669926 scopus 로고
    • Purification and characterization of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue
    • Reichard, U., S. Buttner, H. Eiffert, F. Staib, and R. Ruchel. 1990. Purification and characterization of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue. J. Med. Microbiol. 33:243-251.
    • (1990) J. Med. Microbiol. , vol.33 , pp. 243-251
    • Reichard, U.1    Buttner, S.2    Eiffert, H.3    Staib, F.4    Ruchel, R.5
  • 37
    • 0025280037 scopus 로고
    • Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus
    • Rhodes, J. C., T. W. Amlung, and M. S. Muller. 1990. Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus. Infect. Immun. 58:2529-2534.
    • (1990) Infect. Immun. , vol.58 , pp. 2529-2534
    • Rhodes, J.C.1    Amlung, T.W.2    Muller, M.S.3
  • 41
    • 0015859265 scopus 로고
    • Isolation and crystallization of microbial alkaline protease inhibitor, S-SI
    • Sato, S., and S. Murao. 1973. Isolation and crystallization of microbial alkaline protease inhibitor, S-SI. Agric. Biol. Chem. 37:1067-1074.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1067-1074
    • Sato, S.1    Murao, S.2
  • 42
    • 0025965137 scopus 로고
    • Anaerobic growth of Salmonella typhimurium results in increased uptake by Henle 407 epithelial and mouse peritoneal cells in vitro and repression of a major outer membrane protein
    • Schiemann, D. A., and S. R. Shope. 1991. Anaerobic growth of Salmonella typhimurium results in increased uptake by Henle 407 epithelial and mouse peritoneal cells in vitro and repression of a major outer membrane protein. Infect. Immun. 59:437-440.
    • (1991) Infect. Immun. , vol.59 , pp. 437-440
    • Schiemann, D.A.1    Shope, S.R.2
  • 43
    • 0026750715 scopus 로고
    • Disruption of the Trichoderma reesei cbh2 gene coding for cellobiohydrolase II leads to a delay in the triggering of cellulase formation by cellulose
    • Seiboth, B., R. Messner, F. Gruber, and C. P. Kubicek. 1992. Disruption of the Trichoderma reesei cbh2 gene coding for cellobiohydrolase II leads to a delay in the triggering of cellulase formation by cellulose. J. Gen. Microbiol. 138:1259-1264.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1259-1264
    • Seiboth, B.1    Messner, R.2    Gruber, F.3    Kubicek, C.P.4
  • 44
    • 0028068293 scopus 로고
    • Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli
    • Sirakova, T., A. Markaryan, and P. E. Kolattukudy. 1994. Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli. Infect. Immun. 62:4208-4218.
    • (1994) Infect. Immun. , vol.62 , pp. 4208-4218
    • Sirakova, T.1    Markaryan, A.2    Kolattukudy, P.E.3
  • 45
    • 0024598450 scopus 로고
    • Structure of the cutinase gene and detection of promoter activity in the 5′-flanking region by fungal transformation
    • Soliday, C. L., M. B. Dickman, and P. E. Kolattukudy. 1989. Structure of the cutinase gene and detection of promoter activity in the 5′-flanking region by fungal transformation. J. Bacteriol. 171:1942-1951.
    • (1989) J. Bacteriol. , vol.171 , pp. 1942-1951
    • Soliday, C.L.1    Dickman, M.B.2    Kolattukudy, P.E.3
  • 46
    • 8944234862 scopus 로고
    • Aspergillus proteinases and aspergillosis
    • H. Vanden Bossche, D. W. R. Mackenzie, and G. Cauwenbaergh (ed.), Plenum Press, New York
    • Spitzer, E. D., and G. S. Kobayashi. 1988. Aspergillus proteinases and aspergillosis, p. 129-132. In H. Vanden Bossche, D. W. R. Mackenzie, and G. Cauwenbaergh (ed.), Aspergillus and aspergillosis. Plenum Press, New York.
    • (1988) Aspergillus and Aspergillosis , pp. 129-132
    • Spitzer, E.D.1    Kobayashi, G.S.2
  • 47
    • 0022495143 scopus 로고
    • Elastin and the lung
    • Starcher, B. C. 1986. Elastin and the lung. Thorax 41:577-585.
    • (1986) Thorax , vol.41 , pp. 577-585
    • Starcher, B.C.1
  • 48
    • 0026660149 scopus 로고
    • An Aspergillus fumigatus alkaline protease deficient mutant constructed by gene disruption is deficient in extracellular elastase activity
    • Tang, C. M., J. Cohen, and W. Holden. 1992. An Aspergillus fumigatus alkaline protease deficient mutant constructed by gene disruption is deficient in extracellular elastase activity. Mol. Microbiol. 6:1663-1671.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1663-1671
    • Tang, C.M.1    Cohen, J.2    Holden, W.3
  • 49
    • 0027230493 scopus 로고
    • The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis
    • Tang, C. M., J. Cohen, T. Krausz, S. van Boorden, and D. W. Holden. 1993. The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect. Immun. 61:1650-1656.
    • (1993) Infect. Immun. , vol.61 , pp. 1650-1656
    • Tang, C.M.1    Cohen, J.2    Krausz, T.3    Van Boorden, S.4    Holden, D.W.5
  • 51
    • 0028202878 scopus 로고
    • LasA and lasB genes of Pseudomonas aeruginosa: Analysis of transcription of gene product activity
    • Toder, D. S., S. J. Ferrell, J. L. Nezezon, L. Rust, and B. H. Iglewski. 1994. lasA and lasB genes of Pseudomonas aeruginosa: analysis of transcription of gene product activity. Infect. Immun. 62:1320-1327.
    • (1994) Infect. Immun. , vol.62 , pp. 1320-1327
    • Toder, D.S.1    Ferrell, S.J.2    Nezezon, J.L.3    Rust, L.4    Iglewski, B.H.5
  • 52
    • 0025866289 scopus 로고
    • Pseudomonas aeruginosa LasA: A second elastase under the transcriptional control of lasR
    • Todor, D. S., M. J. Gambello, and B. H. Iglewski. 1991. Pseudomonas aeruginosa LasA: a second elastase under the transcriptional control of lasR. Mol. Microbiol. 5:2003-2010.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2003-2010
    • Todor, D.S.1    Gambello, M.J.2    Iglewski, B.H.3
  • 53
    • 0024540038 scopus 로고
    • Genetic transformation system for the aflatoxin-producing fungus Aspergillus flavus
    • Woloshuk, C. P., E. R. Seip, G. A. Payne, and C. R. Adkins. 1989. Genetic transformation system for the aflatoxin-producing fungus Aspergillus flavus. Appl. Environ. Microbiol. 55:86-90.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 86-90
    • Woloshuk, C.P.1    Seip, E.R.2    Payne, G.A.3    Adkins, C.R.4
  • 54
    • 0025737258 scopus 로고
    • Pseudomonas aeruginosa LasB mutant constructed by insertional mutagenesis reveals elastinolytic activity due to alkaline proteinase and the lasA fragment
    • Wolz, C., E. Hellstern, M. Haug, D. R. Galloway, M. L. Vasil, and G. Doring. 1991. Pseudomonas aeruginosa LasB mutant constructed by insertional mutagenesis reveals elastinolytic activity due to alkaline proteinase and the lasA fragment. Mol. Microbiol. 5:2125-2131.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2125-2131
    • Wolz, C.1    Hellstern, E.2    Haug, M.3    Galloway, D.R.4    Vasil, M.L.5    Doring, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.