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Volumn 9, Issue 3, 1998, Pages 263-269

Molecular genetics of biosurfactant production

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMER; GLYCOLIPID; LIPOPEPTIDE; SURFACTANT;

EID: 0031842019     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80057-8     Document Type: Article
Times cited : (73)

References (61)
  • 1
    • 0030175564 scopus 로고    scopus 로고
    • Biosurfactants: Recent advances
    • Lin SC. Biosurfactants: recent advances. J Chem Technol Biotechnol. 66:1996;109-120.
    • (1996) J Chem Technol Biotechnol , vol.66 , pp. 109-120
    • Lin, S.C.1
  • 2
    • 0030749943 scopus 로고    scopus 로고
    • Microbial production of surfactants and their commercial potential
    • of outstanding interest. This review gives an extensive overview on biosurfactants and covers the structural diversity, fermentative production, and commercial applications.
    • Desai JD, Banat IM. Microbial production of surfactants and their commercial potential. of outstanding interest Microbiol Mol Biol Rev. 61:1997;47-64 This review gives an extensive overview on biosurfactants and covers the structural diversity, fermentative production, and commercial applications.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 47-64
    • Desai, J.D.1    Banat, I.M.2
  • 3
    • 0029980555 scopus 로고    scopus 로고
    • Significance of bacterial surface-active compounds in interaction of bacteria with interfaces
    • Neu T. Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. Microbiol Rev. 60:1996;151-166.
    • (1996) Microbiol Rev , vol.60 , pp. 151-166
    • Neu, T.1
  • 4
    • 0029818809 scopus 로고    scopus 로고
    • Census and consensus in bacterial ecosystems: The LuxR-LuxI family of quorum-sensing transcriptional regulators
    • Fuqua C, Winans SC, Greenberg EP. Census and consensus in bacterial ecosystems: the LuxR-LuxI family of quorum-sensing transcriptional regulators. Annu Rev Microbiol. 50:1996;727-751.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 727-751
    • Fuqua, C.1    Winans, S.C.2    Greenberg, E.P.3
  • 5
    • 0030792814 scopus 로고    scopus 로고
    • Cell-cell communication in gram-positive bacteria
    • of special interest. This review discusses the mechanism of quorum sensing in gram-positive bacteria with a section on Bacillus subtilis.
    • Dunny GM, Leonard BAB. Cell-cell communication in gram-positive bacteria. of special interest Annu Rev Microbiol. 51:1997;527-564 This review discusses the mechanism of quorum sensing in gram-positive bacteria with a section on Bacillus subtilis.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 527-564
    • Dunny, G.M.1    Leonard, B.A.B.2
  • 6
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem M, Quadri LEN, Kuipers OP, de Vos WM. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol Microbiol. 24:1997;895-904.
    • (1997) Mol Microbiol , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.N.2    Kuipers, O.P.3    De Vos, W.M.4
  • 7
    • 33846912675 scopus 로고
    • Dependence of Pseudomonas aeruginosa continuous culture biosurfactant production on nutritional and environmental factors
    • Guerra-Santos LH, Kappeli O, Fiechter A. Dependence of Pseudomonas aeruginosa continuous culture biosurfactant production on nutritional and environmental factors. Appl Microbiol Biotechnol. 24:1986;443-448.
    • (1986) Appl Microbiol Biotechnol , vol.24 , pp. 443-448
    • Guerra-Santos, L.H.1    Kappeli, O.2    Fiechter, A.3
  • 8
    • 0029447852 scopus 로고
    • Rhamnolipid biosurfactant enhancement of hexadecane biodegradation by Pseudomonas aeruginosa
    • Shrive GS, Inguva S, Gunnam S. Rhamnolipid biosurfactant enhancement of hexadecane biodegradation by Pseudomonas aeruginosa. Mol Marine Biol Biotechnol. 4:1995;331-337.
    • (1995) Mol Marine Biol Biotechnol , vol.4 , pp. 331-337
    • Shrive, G.S.1    Inguva, S.2    Gunnam, S.3
  • 9
    • 0029821243 scopus 로고    scopus 로고
    • Inhibition of macrophage phagocytosis by Pseudomonas aeruginosa rhamnolipids in vitro and in vivo
    • McClure C, Schiller N. Inhibition of macrophage phagocytosis by Pseudomonas aeruginosa rhamnolipids in vitro and in vivo. Curr Microbiol. 33:1996;109-117.
    • (1996) Curr Microbiol , vol.33 , pp. 109-117
    • McClure, C.1    Schiller, N.2
  • 10
    • 0002075630 scopus 로고
    • Structure and properties of biosurfactants
    • S. Lang, Wagner F. New York: Marcel Dekker, Inc.
    • Lang S, Wagner F. Structure and properties of biosurfactants. Lang S, Wagner F. Structure and Properties of Biosurfactants. 1987;21-45 Marcel Dekker, Inc. New York.
    • (1987) Structure and Properties of Biosurfactants , pp. 21-45
    • Lang, S.1    Wagner, F.2
  • 11
    • 0000224118 scopus 로고
    • The enzymatic synthesis of a rhamnose-containing glycolipid by extracts of Pseudomonas aeruginosa
    • Burger MM, Glaser L, Burton RM. The enzymatic synthesis of a rhamnose-containing glycolipid by extracts of Pseudomonas aeruginosa. J Biol Chem. 238:1963;2595-2602.
    • (1963) J Biol Chem , vol.238 , pp. 2595-2602
    • Burger, M.M.1    Glaser, L.2    Burton, R.M.3
  • 12
    • 0029160410 scopus 로고
    • Production of Pseudomonas aeruginosa rhamnolipid biosurfactants in heterologous hosts
    • Ochsner UA, Reiser J, Fiechter A, Witholt B. Production of Pseudomonas aeruginosa rhamnolipid biosurfactants in heterologous hosts. Appl Environ Microbiol. 61:1995;3503-3506.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3503-3506
    • Ochsner, U.A.1    Reiser, J.2    Fiechter, A.3    Witholt, B.4
  • 13
    • 0027997539 scopus 로고
    • Isolation, characterization, and expression in Escherichia coli of the Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved in rhamnolipid biosurfactant synthesis
    • Ochsner UA, Fiechter A, Reiser J. Isolation, characterization, and expression in Escherichia coli of the Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved in rhamnolipid biosurfactant synthesis. J Biol Chem. 269:1994;19787-19795.
    • (1994) J Biol Chem , vol.269 , pp. 19787-19795
    • Ochsner, U.A.1    Fiechter, A.2    Reiser, J.3
  • 14
    • 0030930248 scopus 로고    scopus 로고
    • Roles of Pseudomonas aeruginosa las and rhl quorum-sensing systems in control of elastase and rhamnolipid biosynthesis genes
    • of outstanding interest. This paper discusses how the interaction of the two quorum sensing systems influence rhamnolipid production. Single and double mutants were constructed to methodically examine the role of each system on rhamnolipid transcription, verifying that the rhl system regulates rhamnolipid production and the las system regulates the rhl system.
    • Pearson JP, Pesci EC, Iglewski BH. Roles of Pseudomonas aeruginosa las and rhl quorum-sensing systems in control of elastase and rhamnolipid biosynthesis genes. of outstanding interest J Bacteriol. 179:1997;5756-5767 This paper discusses how the interaction of the two quorum sensing systems influence rhamnolipid production. Single and double mutants were constructed to methodically examine the role of each system on rhamnolipid transcription, verifying that the rhl system regulates rhamnolipid production and the las system regulates the rhl system.
    • (1997) J Bacteriol , vol.179 , pp. 5756-5767
    • Pearson, J.P.1    Pesci, E.C.2    Iglewski, B.H.3
  • 15
    • 0024460372 scopus 로고
    • Correlation of nitrogen metabolism with biosurfactant production by Pseudomonas aeruginosa
    • Mulligan CN, Gibbs BF. Correlation of nitrogen metabolism with biosurfactant production by Pseudomonas aeruginosa. Appl Environ Microbiol. 55:1989;3016-3019.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3016-3019
    • Mulligan, C.N.1    Gibbs, B.F.2
  • 16
    • 0029145808 scopus 로고
    • Multiple homologues of LuxR and LuxI control expression of virulence determinants and secondary metabolites through quorum sensing in Pseudomonas aeruginosa PAO1
    • Latifi A, Winson MK, Foglino M, Bycroft BW, Stewart GSAB, Lazdunski A, Williams P. Multiple homologues of LuxR and LuxI control expression of virulence determinants and secondary metabolites through quorum sensing in Pseudomonas aeruginosa PAO1. Mol Microbiol. 17:1995;333-343.
    • (1995) Mol Microbiol , vol.17 , pp. 333-343
    • Latifi, A.1    Winson, M.K.2    Foglino, M.3    Bycroft, B.W.4    Stewart, G.S.A.B.5    Lazdunski, A.6    Williams, P.7
  • 17
    • 0028349371 scopus 로고
    • Isolation and characterization of a regulatory gene affecting rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa
    • Ochsner UA, Koch AK, Fiechter A, Reiser J. Isolation and characterization of a regulatory gene affecting rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa. J Bacteriol. 176:1994;2044-2054.
    • (1994) J Bacteriol , vol.176 , pp. 2044-2054
    • Ochsner, U.A.1    Koch, A.K.2    Fiechter, A.3    Reiser, J.4
  • 18
    • 0029023052 scopus 로고
    • Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa
    • Ochsner UA, Reiser J. Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa. Proc Natl Acad Sci USA. 92:1995;6424-6428.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6424-6428
    • Ochsner, U.A.1    Reiser, J.2
  • 19
    • 0028849833 scopus 로고
    • Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhIR-RhII, another set of regulators in strain PAO1 with homology to the autoinducer-responsive LuxR-LuxI family
    • Brint JM, Ohman DE. Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhIR-RhII, another set of regulators in strain PAO1 with homology to the autoinducer-responsive LuxR-LuxI family. J Bacteriol. 177:1995;7155-7163.
    • (1995) J Bacteriol , vol.177 , pp. 7155-7163
    • Brint, J.M.1    Ohman, D.E.2
  • 22
    • 0029831296 scopus 로고    scopus 로고
    • A hierarchical quorum-sensing cascade in Pseudomonas aeruginosa links the transcriptional activators LasR and RhIR (VsmR) to expression of the stationary-phase sigma factor RpoS
    • Latifi A, Foglino M, Tanaka K, Williams P, Lazdunski A. A hierarchical quorum-sensing cascade in Pseudomonas aeruginosa links the transcriptional activators LasR and RhIR (VsmR) to expression of the stationary-phase sigma factor RpoS. Mol Microbiol. 21:1996;1137-1146.
    • (1996) Mol Microbiol , vol.21 , pp. 1137-1146
    • Latifi, A.1    Foglino, M.2    Tanaka, K.3    Williams, P.4    Lazdunski, A.5
  • 24
    • 0031008226 scopus 로고    scopus 로고
    • The chain of command in Pseudomonas quorum sensing
    • of outstanding interest. This review article covers the hierarchial interactions of the two quorum sensing systems discovered in Pseudomonas aeruginosa.
    • Pesci EC, Iglewski BH. The chain of command in Pseudomonas quorum sensing. of outstanding interest Trends Microbiol. 5:1997;132-134 This review article covers the hierarchial interactions of the two quorum sensing systems discovered in Pseudomonas aeruginosa.
    • (1997) Trends Microbiol , vol.5 , pp. 132-134
    • Pesci, E.C.1    Iglewski, B.H.2
  • 25
    • 0030923758 scopus 로고    scopus 로고
    • Vfr controls quorum sensing in Pseudomonas aeruginosa
    • of special interest. Experiments determined that the cyclic AMP receptor protein binds to the lasR promoter, signifying that the quorum sensing mechanism is partially controlled by cyclic AMP levels in the cell.
    • Albus AM, Pesci EC, Runyen-Janecky LJ, West SEA, Iglewski BH. Vfr controls quorum sensing in Pseudomonas aeruginosa. of special interest J Bacteriol. 179:1997;3928-3935 Experiments determined that the cyclic AMP receptor protein binds to the lasR promoter, signifying that the quorum sensing mechanism is partially controlled by cyclic AMP levels in the cell.
    • (1997) J Bacteriol , vol.179 , pp. 3928-3935
    • Albus, A.M.1    Pesci, E.C.2    Runyen-Janecky, L.J.3    West, S.E.A.4    Iglewski, B.H.5
  • 26
    • 0030985995 scopus 로고    scopus 로고
    • Regulation of las and rhl quorum sensing in Pseudomonas aeruginosa
    • of outstanding interest. The hierarchical control of two quorum sensing systems is analyzed using the lacZ reporter construct to monitor expression of each system under various conditions. Results show that the las system both positively and negatively controls activity of the rhl system.
    • Pesci EC, Pearson JP, Seed PC, Iglewski BH. Regulation of las and rhl quorum sensing in Pseudomonas aeruginosa. of outstanding interest J Bacteriol. 179:1997;3127-3132 The hierarchical control of two quorum sensing systems is analyzed using the lacZ reporter construct to monitor expression of each system under various conditions. Results show that the las system both positively and negatively controls activity of the rhl system.
    • (1997) J Bacteriol , vol.179 , pp. 3127-3132
    • Pesci, E.C.1    Pearson, J.P.2    Seed, P.C.3    Iglewski, B.H.4
  • 27
    • 0030789050 scopus 로고    scopus 로고
    • Regulation of the xcp secretion pathway by multiple quorum-sensing modulons in Pseudomonas aeruginosa
    • Chapon-Herve V, Akrim M, Latifi A, Williams P, Lazdunski A, Bally M. Regulation of the xcp secretion pathway by multiple quorum-sensing modulons in Pseudomonas aeruginosa. Mol Microbiol. 24:1997;1169-1178.
    • (1997) Mol Microbiol , vol.24 , pp. 1169-1178
    • Chapon-Herve, V.1    Akrim, M.2    Latifi, A.3    Williams, P.4    Lazdunski, A.5    Bally, M.6
  • 28
    • 0001925852 scopus 로고
    • Peptide antibiotics
    • P. Zuber, M.M. Nakano, Marahiel M.A. Washington, DC: American Society for Microbiology
    • Zuber P, Nakano MM, Marahiel MA. Peptide antibiotics. Zuber P, Nakano MM, Marahiel MA. Bacillus subtilis and Other Gram-Positive Bacteria. 1993;897-916 American Society for Microbiology, Washington, DC.
    • (1993) Bacillus Subtilis and Other Gram-Positive Bacteria , pp. 897-916
    • Zuber, P.1    Nakano, M.M.2    Marahiel, M.A.3
  • 29
    • 0031234420 scopus 로고    scopus 로고
    • Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis
    • Vollenbroich D, Ozel M, Vater J, Kamp RM, Pauli G. Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis. Biologicals. 25:1997;289-297.
    • (1997) Biologicals , vol.25 , pp. 289-297
    • Vollenbroich, D.1    Ozel, M.2    Vater, J.3    Kamp, R.M.4    Pauli, G.5
  • 30
    • 0030928303 scopus 로고    scopus 로고
    • Application of response-surface methodology to evaluate the optimal environmental conditions for the enhanced production of surfactin
    • Sen R, Swaminathan T. Application of response-surface methodology to evaluate the optimal environmental conditions for the enhanced production of surfactin. Appl Microbiol Biotechnol. 47:1997;358-363.
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 358-363
    • Sen, R.1    Swaminathan, T.2
  • 31
    • 0019403930 scopus 로고
    • Enhanced production of surfactin from Bacillus subtilis by continuous product removal and metal cation additions
    • Cooper DG, MacDonald CR, Duff SJB, Kosaric N. Enhanced production of surfactin from Bacillus subtilis by continuous product removal and metal cation additions. Appl Environ Microbiol. 42:1981;408-412.
    • (1981) Appl Environ Microbiol , vol.42 , pp. 408-412
    • Cooper, D.G.1    MacDonald, C.R.2    Duff, S.J.B.3    Kosaric, N.4
  • 32
    • 84948644832 scopus 로고
    • Determination of fatty acid in surfactin and elucidation of the total structure of surfactin
    • Kakinuma A, Sugino H, Isono M, Tamura G, Arima K. Determination of fatty acid in surfactin and elucidation of the total structure of surfactin. Agr Biol Chem. 33:1969;973-976.
    • (1969) Agr Biol Chem , vol.33 , pp. 973-976
    • Kakinuma, A.1    Sugino, H.2    Isono, M.3    Tamura, G.4    Arima, K.5
  • 34
    • 0027458001 scopus 로고
    • Structural and functional organization of the surfactin synthetase multienzyme system
    • Menkhaus M, Ullrich C, Kluge B, Vater J, Vollenbroich D, Kamp RM. Structural and functional organization of the surfactin synthetase multienzyme system. J Biol Chem. 268:1993;7678-7684.
    • (1993) J Biol Chem , vol.268 , pp. 7678-7684
    • Menkhaus, M.1    Ullrich, C.2    Kluge, B.3    Vater, J.4    Vollenbroich, D.5    Kamp, R.M.6
  • 35
    • 0028965286 scopus 로고
    • Analysis of errors in finished DNA sequences: The surfactin operon of Bacillus subtilis as an example
    • Fabret C, Quentin Y, Guiseppi A, Busuttil J, Haiech J, Denizot F. Analysis of errors in finished DNA sequences: the surfactin operon of Bacillus subtilis as an example. Microbiology. 141:1995;345-350.
    • (1995) Microbiology , vol.141 , pp. 345-350
    • Fabret, C.1    Quentin, Y.2    Guiseppi, A.3    Busuttil, J.4    Haiech, J.5    Denizot, F.6
  • 36
    • 0028837014 scopus 로고
    • Modular structure of genes encoding multifunctional peptide synthases required for non-ribosomal peptide synthesis
    • Stachelhaus T, Marahiel MA. Modular structure of genes encoding multifunctional peptide synthases required for non-ribosomal peptide synthesis. FEMS Microbiol Lett. 125:1995;3-14.
    • (1995) FEMS Microbiol Lett , vol.125 , pp. 3-14
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 37
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • of outstanding interest. This review explians the genetic organization and biochemical mechanism by which protein synthetases function, using surfactin genetics and production as one of several examples.
    • Marahiel MA. Protein templates for the biosynthesis of peptide antibiotics. of outstanding interest Chem Biol. 4:1997;561-567 This review explians the genetic organization and biochemical mechanism by which protein synthetases function, using surfactin genetics and production as one of several examples.
    • (1997) Chem Biol , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 39
    • 0030798978 scopus 로고    scopus 로고
    • Engineering of peptide synthetases. Key role of the thioesterase-like domain for efficient production of recombinant peptides
    • of special interest. The authors genetically modify the surfactin peptide synthetase. The significance of this work is that the peptide synthetases can be genetically modified to create novel structures.
    • de Ferra F, Rodriguez F, Tortora O, Tosi C, Grandi G. Engineering of peptide synthetases. Key role of the thioesterase-like domain for efficient production of recombinant peptides. of special interest J Biol Chem. 272:1997;25304-25309 The authors genetically modify the surfactin peptide synthetase. The significance of this work is that the peptide synthetases can be genetically modified to create novel structures.
    • (1997) J Biol Chem , vol.272 , pp. 25304-25309
    • De Ferra, F.1    Rodriguez, F.2    Tortora, O.3    Tosi, C.4    Grandi, G.5
  • 40
    • 0026520361 scopus 로고
    • Isolation and characterization of sfp: A gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis
    • Nakano MM, Corbell N, Besson J, Zuber P. Isolation and characterization of sfp: a gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis. Mol Gen Genet. 232:1992;313-321.
    • (1992) Mol Gen Genet , vol.232 , pp. 313-321
    • Nakano, M.M.1    Corbell, N.2    Besson, J.3    Zuber, P.4
  • 42
    • 0028145628 scopus 로고
    • Identification of comS, a gene of the srfA operon that regulates the establishment of genetic competence in Bacillus subtilis
    • D'Souza C, Nakano MM, Zuber P. Identification of comS, a gene of the srfA operon that regulates the establishment of genetic competence in Bacillus subtilis. Proc Natl Acad Sci USA. 91:1994;9397-9401.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9397-9401
    • D'Souza, C.1    Nakano, M.M.2    Zuber, P.3
  • 43
    • 0028964280 scopus 로고
    • A small gene, designated comS, located within the coding region of the fourth amino acid-activation domain of srfA, is required for competence development in Bacillus subtilis
    • Hamoen LW, Eshuis H, Jongbloed J, Venema G, van Sinderen D. A small gene, designated comS, located within the coding region of the fourth amino acid-activation domain of srfA, is required for competence development in Bacillus subtilis. Mol Microbiol. 15:1995;55-63.
    • (1995) Mol Microbiol , vol.15 , pp. 55-63
    • Hamoen, L.W.1    Eshuis, H.2    Jongbloed, J.3    Venema, G.4    Van Sinderen, D.5
  • 44
    • 0029974543 scopus 로고    scopus 로고
    • Who's competent and when: Regulation of natural genetic competence in bacteria
    • Solomon JM, Grossman AD. Who's competent and when: regulation of natural genetic competence in bacteria. Trends Genet. 12:1996;150-155.
    • (1996) Trends Genet , vol.12 , pp. 150-155
    • Solomon, J.M.1    Grossman, A.D.2
  • 45
    • 0028284877 scopus 로고
    • Biochemical and genetic characterization of a competence pheromone from B. subtilis
    • Magnuson R, Solomon J, Grossman AD. Biochemical and genetic characterization of a competence pheromone from B. subtilis. Cell. 77:1994;207-216.
    • (1994) Cell , vol.77 , pp. 207-216
    • Magnuson, R.1    Solomon, J.2    Grossman, A.D.3
  • 46
    • 0029959768 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular peptide factor that affects two different development pathways in Bacillus subtilis
    • Solomon JM, Lazazzera BA, Grossman AD. Purification and characterization of an extracellular peptide factor that affects two different development pathways in Bacillus subtilis. Genes Dev. 10:1996;2014-2024.
    • (1996) Genes Dev , vol.10 , pp. 2014-2024
    • Solomon, J.M.1    Lazazzera, B.A.2    Grossman, A.D.3
  • 47
    • 0027318149 scopus 로고
    • Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis
    • Nakano MM, Zuber P. Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis. J Bacteriol. 175:1993;3188-3191.
    • (1993) J Bacteriol , vol.175 , pp. 3188-3191
    • Nakano, M.M.1    Zuber, P.2
  • 48
    • 0030830216 scopus 로고    scopus 로고
    • An exported peptide functions intracellularly to contribute to cell density signaling in B. subtilis
    • Lazazzera BA, Solomon JM, Grossman AD. An exported peptide functions intracellularly to contribute to cell density signaling in B. subtilis. Cell. 89:1997;917-925.
    • (1997) Cell , vol.89 , pp. 917-925
    • Lazazzera, B.A.1    Solomon, J.M.2    Grossman, A.D.3
  • 49
    • 0030047027 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis
    • Luttinger A, Hahn J, Dubnau D. Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis. Mol Microbiol. 19:1996;343-356.
    • (1996) Mol Microbiol , vol.19 , pp. 343-356
    • Luttinger, A.1    Hahn, J.2    Dubnau, D.3
  • 50
    • 0029813127 scopus 로고    scopus 로고
    • Plasmid-amplified comS enhances genetic competence and suppresses sinR in Bacillus subtilis
    • Liu L, Nakano MM, Lee OH, Zuber P. Plasmid-amplified comS enhances genetic competence and suppresses sinR in Bacillus subtilis. J Bacteriol. 178:1996;5144-5152.
    • (1996) J Bacteriol , vol.178 , pp. 5144-5152
    • Liu, L.1    Nakano, M.M.2    Lee, O.H.3    Zuber, P.4
  • 51
    • 0029016528 scopus 로고
    • Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50
    • Yakimov MM, Timmis KN, Wray V, Fredrickson HL. Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50. Appl Environ Microbiol. 61:1995;1706-1713.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1706-1713
    • Yakimov, M.M.1    Timmis, K.N.2    Wray, V.3    Fredrickson, H.L.4
  • 52
    • 0031278570 scopus 로고    scopus 로고
    • ComA-dependent transcriptional activation of lichenysin A synthetase promoter in Bacillus subtilis cells
    • Yakimov MM, Golyshin PN. ComA-dependent transcriptional activation of lichenysin A synthetase promoter in Bacillus subtilis cells. Biotechnol Prog. 13:1997;757-761.
    • (1997) Biotechnol Prog , vol.13 , pp. 757-761
    • Yakimov, M.M.1    Golyshin, P.N.2
  • 53
    • 0345486872 scopus 로고
    • Adhesion and desorption during the growth of Acinetobacter calcoaceticus on hydrocarbons
    • E. Rosenberg, M. Rosenberg, Y. Shoham, N. Kaplan, Sar N. Washington, DC: American Society for Microbiology
    • Rosenberg E, Rosenberg M, Shoham Y, Kaplan N, Sar N. Adhesion and desorption during the growth of Acinetobacter calcoaceticus on hydrocarbons. Rosenberg E, Rosenberg M, Shoham Y, Kaplan N, Sar N. Adhesion and Desorption During the Growth of Acinetobacter Calcoaceticus on Hydrocarbons. 1989;219-227 American Society for Microbiology, Washington, DC.
    • (1989) Adhesion and Desorption during the Growth of Acinetobacter Calcoaceticus on Hydrocarbons , pp. 219-227
    • Rosenberg, E.1    Rosenberg, M.2    Shoham, Y.3    Kaplan, N.4    Sar, N.5
  • 54
    • 0021953149 scopus 로고
    • Exocellular esterase and emulsan release from the cell surface of Acinetobacter calcoaceticus
    • Shabtai Y, Gutnick DL. Exocellular esterase and emulsan release from the cell surface of Acinetobacter calcoaceticus. J Bacteriol. 161:1985;1176-1181.
    • (1985) J Bacteriol , vol.161 , pp. 1176-1181
    • Shabtai, Y.1    Gutnick, D.L.2
  • 55
    • 0024573670 scopus 로고
    • Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1
    • Reddy PG, Allon R, Mevarech M, Mendelovitz S, Sato Y, Gutnick DL. Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1. Gene. 76:1989;145-152.
    • (1989) Gene , vol.76 , pp. 145-152
    • Reddy, P.G.1    Allon, R.2    Mevarech, M.3    Mendelovitz, S.4    Sato, Y.5    Gutnick, D.L.6
  • 56
    • 85046520109 scopus 로고
    • Esterase from the oil-degrading Acinetobacter Iwoffii RAG-1: Sequence analysis and over-expression in Escherichia coli
    • Alon RN, Gutnick DL. Esterase from the oil-degrading Acinetobacter Iwoffii RAG-1: sequence analysis and over-expression in Escherichia coli. FEMS Microbiol Lett. 112:1993;275-280.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 275-280
    • Alon, R.N.1    Gutnick, D.L.2
  • 57
    • 0345361385 scopus 로고
    • Role of lipase in the emulsification of hydrocarbons by Acinetobacter calcoaceticus RAG-1
    • Baltimore, MD: University of Maryland
    • Leahy JG. Role of lipase in the emulsification of hydrocarbons by Acinetobacter calcoaceticus RAG-1. PhD Thesis. 1993;University of Maryland, Baltimore, MD.
    • (1993) PhD Thesis
    • Leahy, J.G.1
  • 58
    • 0344498974 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the lipase and lipase chaperone from Acinetobacter calcoaceticus RAG-1, and redefinition of a proteobacterial lipase family and an analogous lipase chaperone family
    • in press
    • Sullivan ER, Leahy JG, Colwell RR. Cloning and sequence analysis of the lipase and lipase chaperone from Acinetobacter calcoaceticus RAG-1, and redefinition of a proteobacterial lipase family and an analogous lipase chaperone family. Microbiology. 1998;. in press.
    • (1998) Microbiology
    • Sullivan, E.R.1    Leahy, J.G.2    Colwell, R.R.3
  • 59
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • Stachelhaus T, Schneider A, Marahiel MA. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science. 269:1995;69-72.
    • (1995) Science , vol.269 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 60
    • 0031105254 scopus 로고    scopus 로고
    • Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with a phosphopantetheinyl transferase
    • Ku J, Mirmira RG, Liu L, Santi DV. Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with a phosphopantetheinyl transferase. Chem Biol. 4:1997;203-207.
    • (1997) Chem Biol , vol.4 , pp. 203-207
    • Ku, J.1    Mirmira, R.G.2    Liu, L.3    Santi, D.V.4


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