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Volumn 115, Issue 4, 2013, Pages 394-404

Random mutagenesis of atfA and screening for Acinetobacter baylyi mutants with an altered lipid accumulation

Author keywords

Acinetobacter baylyi; Random mutagenesis; TAGs; Wax esters; WS DGAT

Indexed keywords

ACINETOBACTER BAYLYI; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SIMMONDSIA;

EID: 84876073410     PISSN: 14387697     EISSN: 14389312     Source Type: Journal    
DOI: 10.1002/ejlt.201200401     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 0015130119 scopus 로고
    • Occurrence of waxes in Acinetobacter
    • Gallagher, I. H. C., Occurrence of waxes in Acinetobacter. J. Gen. Microbiol. 1971, 68, 245-247.
    • (1971) J. Gen. Microbiol. , vol.68 , pp. 245-247
    • Gallagher, I.H.C.1
  • 2
    • 0037424538 scopus 로고    scopus 로고
    • A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase mediates wax ester and triacylglycerol biosynthesis in Acinetobacter calcoaceticus ADP1
    • Kalscheuer, R., Steinbüchel, A., A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase mediates wax ester and triacylglycerol biosynthesis in Acinetobacter calcoaceticus ADP1. J. Biol. Chem. 2003, 278, 8075-8082.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8075-8082
    • Kalscheuer, R.1    Steinbüchel, A.2
  • 3
    • 3242750587 scopus 로고    scopus 로고
    • Introduction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture
    • Daniel, J., Deb, C., Dubey, V. S., Sirakova, T. D. et al., Introduction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture. J. Bacteriol. 2004, 186, 5017-5030.
    • (2004) J. Bacteriol. , vol.186 , pp. 5017-5030
    • Daniel, J.1    Deb, C.2    Dubey, V.S.3    Sirakova, T.D.4
  • 4
    • 34248384746 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoid wax ester in Marinobacter hydrocarbonoclasticus DSM 8798: Identification and characterization of isoprenoid coenzyme A synthetase and wax ester synthases
    • Holtzapple, E., Schmidt-Dannert, C., Biosynthesis of isoprenoid wax ester in Marinobacter hydrocarbonoclasticus DSM 8798: Identification and characterization of isoprenoid coenzyme A synthetase and wax ester synthases. J. Bacteriol. 2007, 189, 3804-3812.
    • (2007) J. Bacteriol. , vol.189 , pp. 3804-3812
    • Holtzapple, E.1    Schmidt-Dannert, C.2
  • 5
    • 33846630830 scopus 로고    scopus 로고
    • Analysis of storage lipid accumulation in Alcanivorax borkumensis: Evidence for alternative triacylglycerol biosynthesis routes in bacteria
    • Kalscheuer, R., Stöveken, T., Malkus, U., Reichelt, R. et al., Analysis of storage lipid accumulation in Alcanivorax borkumensis: Evidence for alternative triacylglycerol biosynthesis routes in bacteria. J. Bacteriol. 2007, 189, 918-928.
    • (2007) J. Bacteriol. , vol.189 , pp. 918-928
    • Kalscheuer, R.1    Stöveken, T.2    Malkus, U.3    Reichelt, R.4
  • 6
    • 51149089101 scopus 로고    scopus 로고
    • Cloning and characterization of a gene involved in triacylglycerol biosynthesis and identification of additional homologous genes in the oleaginous bacterium Rhodococcus opacus PD630
    • Alvarez, A. F., Alvarez, H. M., Kalscheuer, R., Wältermann, M., Steinbüchel, A., Cloning and characterization of a gene involved in triacylglycerol biosynthesis and identification of additional homologous genes in the oleaginous bacterium Rhodococcus opacus PD630. Microbiology 2008, 154, 2327-2335.
    • (2008) Microbiology , vol.154 , pp. 2327-2335
    • Alvarez, A.F.1    Alvarez, H.M.2    Kalscheuer, R.3    Wältermann, M.4    Steinbüchel, A.5
  • 8
    • 68349093972 scopus 로고    scopus 로고
    • Analysis of neutral lipid biosynthesis in Streptomyces avermitilis MA-4680 and characterization of an acyltransferase involved herein
    • Kaddor, C., Biermann, K., Kalscheuer, R., Steinbüchel, A., Analysis of neutral lipid biosynthesis in Streptomyces avermitilis MA-4680 and characterization of an acyltransferase involved herein. Appl. Microbiol. Biotechnol. 2009, 84, 143-155.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 143-155
    • Kaddor, C.1    Biermann, K.2    Kalscheuer, R.3    Steinbüchel, A.4
  • 9
    • 34250025178 scopus 로고    scopus 로고
    • Cuticular wax biosynthesis in petunia petals: Cloning and characterization of an alcohol-acyltransferase that synthesizes wax-esters
    • King, A., Nam, J. W., Han, J., Hilliard, J., Jaworski, J. G., Cuticular wax biosynthesis in petunia petals: Cloning and characterization of an alcohol-acyltransferase that synthesizes wax-esters. Planta 2007, 226, 381-394.
    • (2007) Planta , vol.226 , pp. 381-394
    • King, A.1    Nam, J.W.2    Han, J.3    Hilliard, J.4    Jaworski, J.G.5
  • 10
    • 55549115700 scopus 로고    scopus 로고
    • Identification of the wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis
    • Li, F., Wu, X., Lam, P., Bird, D. et al., Identification of the wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis. Plant Physiol. 2008, 148, 97-107.
    • (2008) Plant Physiol. , vol.148 , pp. 97-107
    • Li, F.1    Wu, X.2    Lam, P.3    Bird, D.4
  • 11
    • 33846477310 scopus 로고    scopus 로고
    • Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA:diacylglycerol acyltransferases
    • Wältermann, M., Stöveken, T., Steinbüchel, A., Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA:diacylglycerol acyltransferases. Biochimie 2007, 89, 230-242.
    • (2007) Biochimie , vol.89 , pp. 230-242
    • Wältermann, M.1    Stöveken, T.2    Steinbüchel, A.3
  • 12
    • 53149087861 scopus 로고    scopus 로고
    • Acyltransferases in bacterial glycerophospholipid synthesis
    • Zhang, Y. M., Rock, C. O., Acyltransferases in bacterial glycerophospholipid synthesis. J. Lipid Res. 2008, 49, 1867-1874.
    • (2008) J. Lipid Res. , vol.49 , pp. 1867-1874
    • Zhang, Y.M.1    Rock, C.O.2
  • 14
  • 15
    • 68349111234 scopus 로고    scopus 로고
    • Both histidine residues of the conserved HHXXXDG motif are essential for wax ester synthase/acyl-CoA:diacylglycerol acyl-transferase catalysis
    • Stöveken, T., Kalscheuer, R., Steinbüchel, A., Both histidine residues of the conserved HHXXXDG motif are essential for wax ester synthase/acyl-CoA:diacylglycerol acyl-transferase catalysis. Eur. J. Lipid Sci. Technol. 2009, 111, 112-119.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 112-119
    • Stöveken, T.1    Kalscheuer, R.2    Steinbüchel, A.3
  • 17
    • 0033765914 scopus 로고    scopus 로고
    • Purification of a jojoba embryo wax synthase, cloning of its cDNA, and production of high levels of wax in seeds of transgenic Arabidopsis
    • Lardizabal, K. D., Metz, J. G., Sakamoto, T., Hutton, W. C. et al., Purification of a jojoba embryo wax synthase, cloning of its cDNA, and production of high levels of wax in seeds of transgenic Arabidopsis. Plant Physiol. 2000, 122, 645-655.
    • (2000) Plant Physiol. , vol.122 , pp. 645-655
    • Lardizabal, K.D.1    Metz, J.G.2    Sakamoto, T.3    Hutton, W.C.4
  • 18
    • 0242298277 scopus 로고    scopus 로고
    • Industrial use of lipases to produce fatty acid esters
    • Hills, G., Industrial use of lipases to produce fatty acid esters. Eur. J. Lipid Sci. Technol. 2003, 105, 601-607.
    • (2003) Eur. J. Lipid Sci. Technol. , vol.105 , pp. 601-607
    • Hills, G.1
  • 19
    • 33144479544 scopus 로고    scopus 로고
    • Neutral lipid biosynthesis in engineered Escherichia coli: Jojoba oil-like wax esters and fatty acid butyl esters
    • Kalscheuer, R., Stöveken, T., Luftmann, H., Malkus, U. et al., Neutral lipid biosynthesis in engineered Escherichia coli: Jojoba oil-like wax esters and fatty acid butyl esters. Appl. Environ. Microbiol. 2006, 72, 1373-1379.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1373-1379
    • Kalscheuer, R.1    Stöveken, T.2    Luftmann, H.3    Malkus, U.4
  • 20
    • 45549087079 scopus 로고    scopus 로고
    • Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels
    • Steinbüchel, A., Stöveken, T., Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels. Angew. Chem. Int. Ed. Engl. 2008, 47, 3688-3694.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 3688-3694
    • Steinbüchel, A.1    Stöveken, T.2
  • 21
    • 33748762752 scopus 로고    scopus 로고
    • Microdiesel: Escherichia coli engineered for fuel production
    • Kalscheuer, R., Stölting, T., Steinbüchel, A., Microdiesel: Escherichia coli engineered for fuel production. Microbiology (SGM) 2006, 152, 2529-2536.
    • (2006) Microbiology (SGM) , vol.152 , pp. 2529-2536
    • Kalscheuer, R.1    Stölting, T.2    Steinbüchel, A.3
  • 22
  • 24
    • 0001038052 scopus 로고
    • Formation and utilization of poly-beta-hydroxybutyric acid by knallgas bacteria (Hydrogenomonas)
    • Schlegel, H. G., Gottschalk, G., von Bartha, R., Formation and utilization of poly-beta-hydroxybutyric acid by knallgas bacteria (Hydrogenomonas). Nature 1961, 191, 463-465.
    • (1961) Nature , vol.191 , pp. 463-465
    • Schlegel, H.G.1    Gottschalk, G.2    von Bartha, R.3
  • 25
    • 0032693153 scopus 로고    scopus 로고
    • Biotransformation of eugenol to vanillin by a mutant of Pseudomonas sp. strain HR199 constructed by disruption of the vanillin dehydrogenase (vdh) gene
    • Overhage, J., Priefert, H., Rabenhorst, J., Steinbüchel, A., Biotransformation of eugenol to vanillin by a mutant of Pseudomonas sp. strain HR199 constructed by disruption of the vanillin dehydrogenase (vdh) gene. Appl. Microbiol. Biotechnol. 1999, 52, 820-828.
    • (1999) Appl. Microbiol. Biotechnol. , vol.52 , pp. 820-828
    • Overhage, J.1    Priefert, H.2    Rabenhorst, J.3    Steinbüchel, A.4
  • 26
    • 0027465204 scopus 로고
    • Physiological characterization of natural transformation in Acinetobacter calcoaceticus
    • Palmen, R., Vosman, B., Buijsman, P., Breek, C. K. D., Hellingwerf, K. J., Physiological characterization of natural transformation in Acinetobacter calcoaceticus. J. Gen. Microbiol. 1993, 139, 295-305.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 295-305
    • Palmen, R.1    Vosman, B.2    Buijsman, P.3    Breek, C.K.D.4    Hellingwerf, K.J.5
  • 27
    • 0025349477 scopus 로고
    • Analysis and nucleotide sequence of an origin of DNA replication in Acinetobacter calcoaceticus and its use for Escherichia coli shuttle plasmids
    • Hunger, M., Schmucker, R., Kishan, V., Hillen, W., Analysis and nucleotide sequence of an origin of DNA replication in Acinetobacter calcoaceticus and its use for Escherichia coli shuttle plasmids. Gene 1990, 87, 45-51.
    • (1990) Gene , vol.87 , pp. 45-51
    • Hunger, M.1    Schmucker, R.2    Kishan, V.3    Hillen, W.4
  • 28
    • 0029815077 scopus 로고    scopus 로고
    • Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: Fatty acid repression of lipA expression and degradation of LipA
    • Kok, R. G., Nudel, C. B., Gonzalez, R. H., Nugteren-Roodzant, I. M., Hellingwerf, K. J., Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: Fatty acid repression of lipA expression and degradation of LipA. J. Bacteriol. 1996, 178, 6025-6035.
    • (1996) J. Bacteriol. , vol.178 , pp. 6025-6035
    • Kok, R.G.1    Nudel, C.B.2    Gonzalez, R.H.3    Nugteren-Roodzant, I.M.4    Hellingwerf, K.J.5
  • 29
    • 77954735705 scopus 로고    scopus 로고
    • Acinetobacter baylyi starvation-induced genes identified through incubation in long-term stationary phase
    • Lostroh, C. P., Voyles, B. A., Acinetobacter baylyi starvation-induced genes identified through incubation in long-term stationary phase. Appl. Environ. Microbiol. 2010, 76, 4905-4908.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4905-4908
    • Lostroh, C.P.1    Voyles, B.A.2
  • 30
    • 0029872743 scopus 로고    scopus 로고
    • The expression of the Acinetobacter calcoaceticus recA gene increases in response to DNA damage independently of RecA and of development of competence for natural transformation
    • Rauch, P. J. G., Palmen, R., Burds, A. A., Gregg-Jolly, L. A. et al., The expression of the Acinetobacter calcoaceticus recA gene increases in response to DNA damage independently of RecA and of development of competence for natural transformation. Microbiology (SGM) 1996, 142, 1025-1032.
    • (1996) Microbiology (SGM) , vol.142 , pp. 1025-1032
    • Rauch, P.J.G.1    Palmen, R.2    Burds, A.A.3    Gregg-Jolly, L.A.4
  • 31
    • 0035153271 scopus 로고    scopus 로고
    • Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Trautwein, G., Gerischer, U., Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 2001, 183, 873-881.
    • (2001) J. Bacteriol. , vol.183 , pp. 873-881
    • Trautwein, G.1    Gerischer, U.2
  • 32
    • 84876096450 scopus 로고    scopus 로고
    • Ph. D. Thesis, Westfälische Wilhelms-Universität Münster, Münster (Germany)
    • Kalscheuer, R., Ph. D. Thesis, Westfälische Wilhelms-Universität Münster, Münster (Germany) 2003.
    • (2003)
    • Kalscheuer, R.1
  • 33
    • 0031113943 scopus 로고    scopus 로고
    • An efficient random mutagenesis technique using an E. coli mutator strain
    • Greener, A., Callahan, M., Jerpseth, B., An efficient random mutagenesis technique using an E. coli mutator strain. Mol. Biotechnol. 1997, 7, 189-195.
    • (1997) Mol. Biotechnol. , vol.7 , pp. 189-195
    • Greener, A.1    Callahan, M.2    Jerpseth, B.3
  • 34
    • 2942630097 scopus 로고    scopus 로고
    • Encoded errors: Mutations and rearrangements mediated by misalignment at repetitive DNA sequences
    • Lovett, S. T., Encoded errors: Mutations and rearrangements mediated by misalignment at repetitive DNA sequences. Mol. Microbiol. 2004, 52, 1243-1253.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1243-1253
    • Lovett, S.T.1
  • 35
    • 0023410420 scopus 로고
    • Spectra of spontaneous mutations in Escherichia coli strains defective in mismatch correction: The nature of in vivo DNA replication errors
    • Schaaper, R. M., Dunn, R. L., Spectra of spontaneous mutations in Escherichia coli strains defective in mismatch correction: The nature of in vivo DNA replication errors. Proc. Natl. Acad. Sci. USA 1987, 84, 6220-6224.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6220-6224
    • Schaaper, R.M.1    Dunn, R.L.2
  • 36
    • 10444228204 scopus 로고    scopus 로고
    • Synthesis of novel lipids in Saccharomyces cerevisiae by heterologous expression of an unspecific bacterial acyltransferase
    • Kalscheuer, R., Luftmann, H., Steinbüchel, A., Synthesis of novel lipids in Saccharomyces cerevisiae by heterologous expression of an unspecific bacterial acyltransferase. Appl. Environ. Microbiol. 2004, 70, 7112-7125.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 7112-7125
    • Kalscheuer, R.1    Luftmann, H.2    Steinbüchel, A.3
  • 37
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., Barber, J. D., Barton, G. J., The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 2008, 36, W197- W201.
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 38
    • 17444424974 scopus 로고    scopus 로고
    • The structure of α-helical coiled coils
    • Lupas, A. N., Gruber, M., The structure of α-helical coiled coils. Adv. Protein Chem. 2005, 70, 37-78.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 39
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • Mason, J. M., Arndt, K. M., Coiled coil domains: Stability, specificity, and biological implications. ChemBioChem 2004, 5, 170-176.
    • (2004) ChemBioChem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 41
    • 14544268951 scopus 로고    scopus 로고
    • The wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1: Characterization of a novel type of acyltransferase
    • Stöveken, T., Kalscheuer, R., Malkus, U., Reichelt, R., Steinbüchel, A., The wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1: Characterization of a novel type of acyltransferase. J. Bacteriol. 2005, 187, 1369-1376.
    • (2005) J. Bacteriol. , vol.187 , pp. 1369-1376
    • Stöveken, T.1    Kalscheuer, R.2    Malkus, U.3    Reichelt, R.4    Steinbüchel, A.5
  • 42
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modeling
    • Arnold, K., Bordoli, L., Kopp, J., Schwede, T., The SWISS-MODEL workspace: A web-based environment for protein structure homology modeling. Bioinformatics 2006, 22, 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 44
    • 84857243863 scopus 로고    scopus 로고
    • Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production
    • Shi, S., Valle-Rodríguez, J. O., Khoomrung, S., Siewers, V., Nielsen, J., Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production. Biotechnol. Biofuels 2012, 5, 7-16.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 7-16
    • Shi, S.1    Valle-Rodríguez, J.O.2    Khoomrung, S.3    Siewers, V.4    Nielsen, J.5
  • 45
    • 0024792699 scopus 로고
    • Genetic analysis of protein stability and function
    • Pakula, A. A., Sauer, R. T., Genetic analysis of protein stability and function. Annu. Rev. Genet. 1989, 23, 289-310.
    • (1989) Annu. Rev. Genet. , vol.23 , pp. 289-310
    • Pakula, A.A.1    Sauer, R.T.2


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