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Volumn 75, Issue 12, 2009, Pages 4197-4201

The haloprotease CPI produced by the moderately halophilic bacterium Pseudoalteromonas ruthenica is secreted by the type II secretion pathway

Author keywords

[No Author keywords available]

Indexed keywords

EXTRACELLULAR PROTEASE; GENE ENCODES; HALOPHILIC BACTERIA; METALLOPROTEASES; NUCLEOTIDE SEQUENCES; PSEUDOALTEROMONAS; SEQUENCE SIMILARITY; TYPE II;

EID: 67149134702     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00156-09     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., T. L. Madden, A. A. Schäffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402. (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 3
    • 0024078229 scopus 로고
    • Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene
    • Bever, R. A., and B. H. Iglewski. 1988. Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene. J. Bacteriol. 170:4309-4314.
    • (1988) J. Bacteriol. , vol.170 , pp. 4309-4314
    • Bever, R.A.1    Iglewski, B.H.2
  • 5
    • 0030955131 scopus 로고    scopus 로고
    • Cloning and characterization of the gene (empV) encoding extracellular metalloprotease from Vibrio vulnificus
    • DOI 10.1016/S0378-1119(96)00786-X, PII S037811199600786X
    • Chuang, Y. C., T. M. Chang, and M. C. Chang. 1997. Cloning and characterization of the gene (empV) encoding extracellular metalloprotease from Vibrio vulnificus. Gene 189:163-168. (Pubitemid 27187186)
    • (1997) Gene , vol.189 , Issue.2 , pp. 163-168
    • Chuang, Y.C.1    Chang, T.C.2    Chang, M.C.3
  • 6
    • 0026538941 scopus 로고
    • Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus
    • David, V. A., A. H. Deutch, A. Sloma, D. Pawlyk, A. Ally, and D. R. Durham. 1992. Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. Gene 112:107-112.
    • (1992) Gene , vol.112 , pp. 107-112
    • David, V.A.1    Deutch, A.H.2    Sloma, A.3    Pawlyk, D.4    Ally, A.5    Durham, D.R.6
  • 7
    • 0024341985 scopus 로고
    • Protein secretion by Gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12
    • d'Enfert, C., I. Reyss, C. Wandersman, and A. P. Pugsley. 1989. Protein secretion by Gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12. J. Biol. Chem. 264:17462-17468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17462-17468
    • D'Enfert, C.1    Reyss, I.2    Wandersman, C.3    Pugsley, A.P.4
  • 8
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • DOI 10.1128/JB.187.23.8104-8113.2005
    • Dilks, K., M. I. Giménez, and M. Pohlschröder. 2005. Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J. Bacteriol. 187:8104-8113. (Pubitemid 41691703)
    • (2005) Journal of Bacteriology , vol.187 , Issue.23 , pp. 8104-8113
    • Dilks, K.1    Gimenez, M.I.2    Pohlschroder, M.3
  • 9
    • 38049068849 scopus 로고    scopus 로고
    • Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium sp. AH-6
    • Dodia, M. S., C. M. Rawal, H. G. Bhimani, R. H. Joshi, S. K. Khare, and S. P. Singh. 2008. Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium sp. AH-6. J. Ind. Microbiol. Biotechnol. 35:121-131.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 121-131
    • Dodia, M.S.1    Rawal, C.M.2    Bhimani, H.G.3    Joshi, R.H.4    Khare, S.K.5    Singh, S.P.6
  • 10
    • 0036048808 scopus 로고    scopus 로고
    • Correlation between pigmentation and antifouling compounds produced by Pseudoalteromonas tunicata
    • Egan, S., S. James, C. Holmstrom, and S. Kjelleberg. 2002. Correlation between pigmentation and antifouling compounds produced by Pseudoalteromonas tunicata. Environ. Microbiol. 4:433-442.
    • (2002) Environ. Microbiol. , vol.4 , pp. 433-442
    • Egan, S.1    James, S.2    Holmstrom, C.3    Kjelleberg, S.4
  • 11
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S., and C. A. Boucher. 1994. A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol. Gen. Genet. 243:112-118.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 12
    • 0034199501 scopus 로고    scopus 로고
    • Extracellular protease of Natrialba magadii: Purification and biochemical characterization
    • Giménez, M. I., C. A. Studdert, J. J. Sánchez, and R. E. De Castro. 2000. Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4:181-188.
    • (2000) Extremophiles , vol.4 , pp. 181-188
    • Giménez, M.I.1    Studdert, C.A.2    Sánchez, J.J.3    De Castro, R.E.4
  • 14
    • 15244339561 scopus 로고    scopus 로고
    • Purification and characterization of serine proteinase from a halophilic bacterium, Filobacillus sp. RF2-5
    • Hiraga, K., Y. Nishikata, S. Namwong, S. Tanasupawat, K. Takada, and K. Oda. 2005. Purification and characterization of serine proteinase from a halophilic bacterium, Filobacillus sp. RF2-5. Biosci. Biotechnol. Biochem. 69:38-44.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 38-44
    • Hiraga, K.1    Nishikata, Y.2    Namwong, S.3    Tanasupawat, S.4    Takada, K.5    Oda, K.6
  • 17
    • 0026600442 scopus 로고
    • The Aeromonas hydrophila exeE gene, required both for protein secretion and normal outer membrane biogenesis, is a member of a general secretion pathway
    • Jiang, B., and S. P. Howard. 1992. The Aeromonas hydrophila exeE gene, required both for protein secretion and normal outer membrane biogenesis, is a member of a general secretion pathway. Mol. Microbiol. 6:1351-1361.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1351-1361
    • Jiang, B.1    Howard, S.P.2
  • 18
    • 0016256784 scopus 로고
    • Protease formation by a moderately halophilic Bacillus strain
    • Kamekura, M., and H. Onishi. 1974. Protease formation by a moderately halophilic Bacillus strain. Appl. Microbiol. 27:809-810.
    • (1974) Appl. Microbiol. , vol.27 , pp. 809-810
    • Kamekura, M.1    Onishi, H.2
  • 19
    • 0026541088 scopus 로고
    • Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii
    • Kamekura, M., Y. Seno, M. L. Holmes, and M. L. Dyall-Smith. 1992. Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii. J. Bacteriol. 174:736-742.
    • (1992) J. Bacteriol. , vol.174 , pp. 736-742
    • Kamekura, M.1    Seno, Y.2    Holmes, M.L.3    Dyall-Smith, M.L.4
  • 20
    • 57649225420 scopus 로고    scopus 로고
    • Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis
    • Karbalaei-Heidari, H. R., M. A. Amoozegar, M. Hajighasemi, A. A. Ziaee, and A. Ventosa. 2009. Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J. Ind. Microbiol. Biotechnol. 36:21-27.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 21-27
    • Karbalaei-Heidari, H.R.1    Amoozegar, M.A.2    Hajighasemi, M.3    Ziaee, A.A.4    Ventosa, A.5
  • 21
    • 37549005219 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli
    • Karbalaei-Heidari, H. R., A. A. Ziaee, M. A. Amoozegar, Y. Cheburkin, and N. Budisa. 2008. Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli. Gene 408:196-203.
    • (2008) Gene , vol.408 , pp. 196-203
    • Karbalaei-Heidari, H.R.1    Ziaee, A.A.2    Amoozegar, M.A.3    Cheburkin, Y.4    Budisa, N.5
  • 22
    • 0029065956 scopus 로고
    • Cloning and study of the genetic organization of the exe gene cluster of Aeromonas salmonicida
    • Karlyshev, A. V., and S. MacIntyre. 1995. Cloning and study of the genetic organization of the exe gene cluster of Aeromonas salmonicida. Gene 158:77-82.
    • (1995) Gene , vol.158 , pp. 77-82
    • Karlyshev, A.V.1    MacIntyre, S.2
  • 23
    • 0034084232 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the gene encoding the extracellular metalloprotease of Aeromonas caviae
    • Kawakami, K., C. Toma, and Y. Honma. 2000. Cloning, sequencing and expression of the gene encoding the extracellular metalloprotease of Aeromonas caviae. Microbiol. Immunol. 44:341-347. (Pubitemid 30365817)
    • (2000) Microbiology and Immunology , vol.44 , Issue.5 , pp. 341-347
    • Kawakami, K.1    Toma, C.2    Honma, Y.3
  • 24
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor. II. General properties
    • Kunitz, M. 1947. Crystalline soybean trypsin inhibitor. II. General properties. J. Gen. Physiol. 30:291-310.
    • (1947) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 25
    • 0036615260 scopus 로고    scopus 로고
    • Cloning and characterization of extracellular metal protease gene of the algicidal marine bacterium Pseudoalteromonas sp. strain A28
    • Lee, S. O., J. Kato, K. Nakashima, A. Kuroda, T. Ikeda, N. Takiguchi, and H. Ohtake. 2002. Cloning and characterization of extracellular metal protease gene of the algicidal marine bacterium Pseudoalteromonas sp. strain A28. Biosci. Biotechnol. Biochem. 66:1366-1369.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1366-1369
    • Lee, S.O.1    Kato, J.2    Nakashima, K.3    Kuroda, A.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7
  • 27
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 28
    • 11044223673 scopus 로고    scopus 로고
    • Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities
    • McIver, K. S., E. Kessler, and D. E. Oman. 2004. Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities. Microbiology 150:3969-3977.
    • (2004) Microbiology , vol.150 , pp. 3969-3977
    • McIver, K.S.1    Kessler, E.2    Oman, D.E.3
  • 29
    • 5444268493 scopus 로고    scopus 로고
    • Biotechnological potential of moderately and extremely halophilic microorganisms
    • J. L. Barredo (ed.), Research Signpost, Kerala, India
    • Mellado, E., and A. Ventosa. 2003. Biotechnological potential of moderately and extremely halophilic microorganisms, p. 233-256. In J. L. Barredo (ed.), Microorganisms for health care, food and enzyme production. Research Signpost, Kerala, India.
    • (2003) Microorganisms for Health Care, Food and Enzyme Production , pp. 233-256
    • Mellado, E.1    Ventosa, A.2
  • 30
    • 0026498428 scopus 로고
    • Cloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum
    • Milton, D. L., A. Norqvist, and H. Wolf-Watz. 1992. Cloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum. J. Bacteriol. 174:7235-7244.
    • (1992) J. Bacteriol. , vol.174 , pp. 7235-7244
    • Milton, D.L.1    Norqvist, A.2    Wolf-Watz, H.3
  • 31
    • 0036481383 scopus 로고    scopus 로고
    • Isolation and characterization of the genes encoding two metalloproteases (Mprl and MprII) from a marine bacterium, Alteromonas sp. strain O-7
    • Miyamoto, K., H. Tsujibo, E. Nukui, H. Itoh, Y. Kaidzu, and Y. Inamori. 2002. Isolation and characterization of the genes encoding two metalloproteases (MprI and MprII) from a marine bacterium, Alteromonas sp. strain O-7. Biosci. Biotechnol. Biochem. 66:416-421. (Pubitemid 39251067)
    • (2002) Bioscience, Biotechnology and Biochemistry , vol.66 , Issue.2 , pp. 416-421
    • Miyamoto, K.1    Tsujibo, H.2    Nukui, E.3    Itoh, H.4    Kaidzu, Y.5    Inamori, Y.6
  • 32
    • 0033973889 scopus 로고    scopus 로고
    • Microbial metalloproteases and pathogenesis
    • DOI 10.1016/S1286-4579(00)00280-X
    • Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microbes Infect. 2:91-98. (Pubitemid 30077931)
    • (2000) Microbes and Infection , vol.2 , Issue.1 , pp. 91-98
    • Miyoshi, S.-I.1    Shinoda, S.2
  • 33
    • 33745514465 scopus 로고    scopus 로고
    • A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: Purification and characterization
    • Namwong, S., K. Hiraga, K. Takada, M. Tsunemi, S. Tanasupawat, and K. Oda. 2006. A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization. Biosci. Biotechnol. Biochem. 70:1395-1401.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1395-1401
    • Namwong, S.1    Hiraga, K.2    Takada, K.3    Tsunemi, M.4    Tanasupawat, S.5    Oda, K.6
  • 34
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu, H. C., and L. A. Heppel. 1965. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240:3685-3692.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 35
    • 0032775329 scopus 로고    scopus 로고
    • Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme
    • Nirasawa, S., Y. Nakajima, Z. Zhang, M. Yoshida, and K. Hayashi. 1999. Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme. Biochim. Biophys. Acta 1433:335-342.
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 335-342
    • Nirasawa, S.1    Nakajima, Y.2    Zhang, Z.3    Yoshida, M.4    Hayashi, K.5
  • 36
    • 0014470465 scopus 로고
    • Proteolytic enzymes from extremely halophilic bacteria
    • Norberg, P., and B. Von Hofsten. 1969. Proteolytic enzymes from extremely halophilic bacteria. J. Gen. Microbiol. 55:251-256.
    • (1969) J. Gen. Microbiol. , vol.55 , pp. 251-256
    • Norberg, P.1    Von Hofsten, B.2
  • 37
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., A. S. Gerber, and D. L. Hartl. 1988. Genetic applications of an inverse polymerase chain reaction. Genetics 120:621-623. (Pubitemid 18260496)
    • (1988) Genetics , vol.120 , Issue.3 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 38
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.2
  • 39
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 40
    • 0030976146 scopus 로고    scopus 로고
    • Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria - A review
    • DOI 10.1016/S0378-1119(96)00803-7, PII S0378111996008037
    • Pugsley, A. P., O. Francetic, O. M. Possot, N. Sauvonnet, and K. R. Hardie. 1997. Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria - a review. Gene 192:13-19. (Pubitemid 27267474)
    • (1997) Gene , vol.192 , Issue.1 , pp. 13-19
    • Pugsley, A.P.1    Francetic, O.2    Possot, O.M.3    Sauvonnet, N.4    Hardie, K.R.5
  • 41
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in Gram-negative bacteria
    • DOI 10.1016/0378-1119(93)90611-6
    • Quandt, J., and M. F. Hynes. 1993. Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127:15-21. (Pubitemid 23140440)
    • (1993) Gene , vol.127 , Issue.1 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 42
    • 0027230857 scopus 로고
    • Molecular cloning and characterization of 13 out genes from Erwinia carotovora subspecies carotovora: Genes encoding members of a general secretion pathway (GSP) widespread in Gram-negative bacteria
    • Reeves, P. J., D. Whitcombe, S. Wharam, M. Gibson, G. Allison, N. Bunce, R. Barallon, P. Douglas, V. Mulholland, S. Stevens, D. Walker, and G. P. C. Salmond. 1993. Molecular cloning and characterization of 13 out genes from Erwinia carotovora subspecies carotovora: genes encoding members of a general secretion pathway (GSP) widespread in Gram-negative bacteria. Mol. Microbiol. 8:443-456.
    • (1993) Mol. Microbiol. , vol.8 , pp. 443-456
    • Reeves, P.J.1    Whitcombe, D.2    Wharam, S.3    Gibson, M.4    Allison, G.5    Bunce, N.6    Barallon, R.7    Douglas, P.8    Mulholland, V.9    Stevens, S.10    Walker, D.11    Salmond, G.P.C.12


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