메뉴 건너뛰기




Volumn 156, Issue 1, 2010, Pages 211-219

PssA is required for α-amylase secretion in Antarctic Pseudoalteromonas haloplanktis

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; LIPOPROTEIN; PROTEIN PSSA; UNCLASSIFIED DRUG;

EID: 76849110057     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.032342-0     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0026766423 scopus 로고
    • Isolation and molecular characterization of a novel broad-host-range plasmid from Bordetella bronchiseptica with sequence similarities to plasmids from gram-positive organisms
    • Antoine, R. & Locht, C. (1992). Isolation and molecular characterization of a novel broad-host-range plasmid from Bordetella bronchiseptica with sequence similarities to plasmids from gram-positive organisms. Mol Microbiol 6, 1785-1799.
    • (1992) Mol Microbiol , vol.6 , pp. 1785-1799
    • Antoine, R.1    Locht, C.2
  • 3
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball, G., Chapon-Hervé, V., Bleves, S., Michel, G. & Bally, M. (1999). Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J Bacteriol 181, 382-388.
    • (1999) J Bacteriol , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Hervé, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 4
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A. & Bycroft, M. (2000). The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299, 1113-1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 5
    • 0027981084 scopus 로고
    • Cloning, molecular characterization and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: A dual lysis system of modular design
    • Birkeland, N. K. (1994). Cloning, molecular characterization and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: a dual lysis system of modular design. Can J Microbiol 40, 658-665.
    • (1994) Can J Microbiol , vol.40 , pp. 658-665
    • Birkeland, N.K.1
  • 6
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch, G. L. & Lässle, M. (1999). The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessiays 21, 932-939.
    • (1999) Bioessiays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 7
    • 0037427963 scopus 로고    scopus 로고
    • The general protein secretory pathway: Phylogenetic analyses leading to evolutionary conclusions
    • Cao, T. B. & Saier, M. H., Jr (2003). The general protein secretory pathway: phylogenetic analyses leading to evolutionary conclusions. Biochim Biophys Acta 1609, 115-125.
    • (2003) Biochim Biophys Acta , vol.1609 , pp. 115-125
    • Cao, T.B.1    Saier Jr, M.H.2
  • 8
    • 12344272637 scopus 로고    scopus 로고
    • Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function
    • Carbonnelle, E., He laine, S., Prouvensier, L., Nassif, X. & Pelicic, V. (2005). Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function. Mol Microbiol 55, 54-64.
    • (2005) Mol Microbiol , vol.55 , pp. 54-64
    • Carbonnelle, E.1    He laine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 9
    • 33645467945 scopus 로고    scopus 로고
    • Secretion of psychrophilic alpha-amylase deletion mutants in Pseudoalteromonas haloplanktis TAC125
    • Cusano, A. M., Parrilli, E., Duilio, A., Sannia, G., Marino, G. & Tutino, M. L. (2006a). Secretion of psychrophilic alpha-amylase deletion mutants in Pseudoalteromonas haloplanktis TAC125. FEMS Microbiol Lett 258, 67-71.
    • (2006) FEMS Microbiol Lett , vol.258 , pp. 67-71
    • Cusano, A.M.1    Parrilli, E.2    Duilio, A.3    Sannia, G.4    Marino, G.5    Tutino, M.L.6
  • 10
    • 33846573332 scopus 로고    scopus 로고
    • A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125
    • Cusano, A. M., Parrilli, E., Marino, G. & Tutino, M. L. (2006b). A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125. Microb Cell Fact 5, 40.
    • (2006) Microb Cell Fact , vol.5 , pp. 40
    • Cusano, A.M.1    Parrilli, E.2    Marino, G.3    Tutino, M.L.4
  • 11
  • 12
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea, L. D. & Regan, L. (2003). TPR proteins: the versatile helix. Trendsi Biochem Sci 28, 655-662.
    • (2003) Trendsi Biochem Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 13
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das, A. K., Cohen, P. W. & Barford, D. (1998). The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J 17, 1192-1199.
    • (1998) EMBO J , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 14
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • Desvaux, M., Hébraud, M., Talon, R. & Henderson, I. R. (2009). Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Tirends Microbiol 17, 139-145.
    • (2009) Tirends Microbiol , vol.17 , pp. 139-145
    • Desvaux, M.1    Hébraud, M.2    Talon, R.3    Henderson, I.R.4
  • 15
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23
    • Feller, G., Lonhienne, C., Deroanne, C., Libioulle, J., Van Beeumen, J. & Gerday, C. (1992). Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23. J Biol Chem 267, 5217-5221.
    • (1992) J Biol Chem , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, C.2    Deroanne, C.3    Libioulle, J.4    Van Beeumen, J.5    Gerday, C.6
  • 16
    • 0032524655 scopus 로고    scopus 로고
    • Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis
    • Feller, G., D'Amico, S., Benotmane, A. M., Joly, F., Van Beeumen, J. & Gerday, C. (1998). Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis. J Biol Chem 273, 12109-12115.
    • (1998) J Biol Chem , vol.273 , pp. 12109-12115
    • Feller, G.1    D'Amico, S.2    Benotmane, A.M.3    Joly, F.4    Van Beeumen, J.5    Gerday, C.6
  • 17
    • 0022403875 scopus 로고
    • Cloning and expression of a Bacillus licheniformis alpha-amylase gene in Pseudomonas aeruginosa
    • Filloux, A., Joyet, P., Murgier, M. & Lazdunski, A. (1985). Cloning and expression of a Bacillus licheniformis alpha-amylase gene in Pseudomonas aeruginosa. FEMS Microbiol Lett 30, 203-207.
    • (1985) FEMS Microbiol Lett , vol.30 , pp. 203-207
    • Filloux, A.1    Joyet, P.2    Murgier, M.3    Lazdunski, A.4
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 22
    • 25844462537 scopus 로고    scopus 로고
    • Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125
    • Médigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P. N., Cheung, F., Cruveiller, S., D'Amico, S. & other authors (2005). Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Res 15, 1325-1335
    • (2005) Genome Res , vol.15 , pp. 1325-1335
    • Médigue, C.1    Krin, E.2    Pascal, G.3    Barbe, V.4    Bernsel, A.5    Bertin, P.N.6    Cheung, F.7    Cruveiller, S.8    D'Amico, S.9
  • 23
    • 23344439437 scopus 로고    scopus 로고
    • Methé, B. A., Nelson, K. E., Deming, J. W., Momen, B., Melamud, E., Zhang, X., Moult, J., Madupu, R., Nelson, W. C. & other authors (2005). The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses. Proc Natl Acad Sci U S A 102, 10913-10918.
    • Methé, B. A., Nelson, K. E., Deming, J. W., Momen, B., Melamud, E., Zhang, X., Moult, J., Madupu, R., Nelson, W. C. & other authors (2005). The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses. Proc Natl Acad Sci U S A 102, 10913-10918.
  • 24
    • 0021073779 scopus 로고
    • Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis
    • Norrander, J., Kempe, T. & Messing, J. (1983). Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene 26, 101-106.
    • (1983) Gene , vol.26 , pp. 101-106
    • Norrander, J.1    Kempe, T.2    Messing, J.3
  • 25
    • 21644435298 scopus 로고    scopus 로고
    • Cell-to-cell transfer of bacterial outer membrane lipoproteins
    • Nudleman, E., Wall, D. & Kaiser, D. (2005). Cell-to-cell transfer of bacterial outer membrane lipoproteins. Science 309, 125-127.
    • (2005) Science , vol.309 , pp. 125-127
    • Nudleman, E.1    Wall, D.2    Kaiser, D.3
  • 26
    • 0015327122 scopus 로고
    • Novel method for detection of β-lactamase by using a chromogenic cephalosporin substrate
    • O'Callaghan, C. H., Morris, A., Kirby, S. M. & Shingler, A. H. (1972). Novel method for detection of β-lactamase by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother 1, 283-288.
    • (1972) Antimicrob Agents Chemother , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.H.4
  • 27
    • 84970005706 scopus 로고    scopus 로고
    • Cell engineering of Pseudoalteromonas haloplanktis TAC125: Construction of a mutant strain with reduced exo-proteolytic activity
    • doi:10.1186/ 1475-2859-5-S1-P36
    • Parrilli, E., Cusano, A. M., Giuliani, M. & Tutino, M. L. (2006). Cell engineering of Pseudoalteromonas haloplanktis TAC125: construction of a mutant strain with reduced exo-proteolytic activity. Microb Cell Fact 5(Suppl 1), P36. doi:10.1186/ 1475-2859-5-S1-P36
    • (2006) Microb Cell Fact , vol.5 , Issue.SUPPL. 1
    • Parrilli, E.1    Cusano, A.M.2    Giuliani, M.3    Tutino, M.L.4
  • 28
    • 41549117559 scopus 로고    scopus 로고
    • Heterologous protein expression in psychrophilic hosts
    • Edited by R. Margesin, F. Schinner, J. C. Marx & C. Gerday. Berlin & Heidelberg: Springer
    • Parrilli, E., Duilio, A. & Tutino, M. L. (2008a). Heterologous protein expression in psychrophilic hosts. In Psychrophiles: from Biodiversity to Biotechnology, pp. 365-379. Edited by R. Margesin, F. Schinner, J. C. Marx & C. Gerday. Berlin & Heidelberg: Springer.
    • (2008) Psychrophiles: From Biodiversity to Biotechnology , pp. 365-379
    • Parrilli, E.1    Duilio, A.2    Tutino, M.L.3
  • 29
    • 41549120637 scopus 로고    scopus 로고
    • Development of an improved Pseudoalteromonas haloplanktis TAC125 strain for recombinant protein secretion at low temperature
    • Parrilli, E., De Vizio, D., Cirulli, C. & Tutino, M. L. (2008b). Development of an improved Pseudoalteromonas haloplanktis TAC125 strain for recombinant protein secretion at low temperature. Microb Cell Fact 7, 2.
    • (2008) Microb Cell Fact , vol.7 , pp. 2
    • Parrilli, E.1    De Vizio, D.2    Cirulli, C.3    Tutino, M.L.4
  • 30
    • 63049091436 scopus 로고    scopus 로고
    • General secretory pathway from marine Antarctic Pseudoalteromonas haloplanktis TAC125
    • Parrilli, E., Giuliani, M. & Tutino, M. L. (2009). General secretory pathway from marine Antarctic Pseudoalteromonas haloplanktis TAC125. Marine Genomics 1, 123-128.
    • (2009) Marine Genomics , vol.1 , pp. 123-128
    • Parrilli, E.1    Giuliani, M.2    Tutino, M.L.3
  • 33
    • 13844318282 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda, H. & Matsuyama, S. (2004). Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 1694, IN1-9.
    • (2004) Biochim Biophys Acta , vol.1694
    • Tokuda, H.1    Matsuyama, S.2
  • 34
    • 0035430835 scopus 로고    scopus 로고
    • A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature
    • Tutino, M. L., Duilio, A., Parrilli, E., Remaut, E., Sannia, G. & Marino, G. (2001). A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature. Extremophiles 5, 257-264.
    • (2001) Extremophiles , vol.5 , pp. 257-264
    • Tutino, M.L.1    Duilio, A.2    Parrilli, E.3    Remaut, E.4    Sannia, G.5    Marino, G.6
  • 35
    • 0036786895 scopus 로고    scopus 로고
    • Secretion of α-amylase from Pseudoalteromonas haloplanktis TAB23: Two different pathways in different hosts
    • Tutino, M. L., Parrilli, E., Giaquinto, L., Duilio, A., Sannia, G., Feller, G. & Marino, G. (2002). Secretion of α-amylase from Pseudoalteromonas haloplanktis TAB23: two different pathways in different hosts. J Bacteriol 184, 5814-5817.
    • (2002) J Bacteriol , vol.184 , pp. 5814-5817
    • Tutino, M.L.1    Parrilli, E.2    Giaquinto, L.3    Duilio, A.4    Sannia, G.5    Feller, G.6    Marino, G.7
  • 36
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - an integration platform for the signature recognition methods in InterPro
    • Zdobnov, E. M. & Apweiler, R. (2001). InterProScan - an integration platform for the signature recognition methods in InterPro. Bioinformatics 17, 847-848.
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.