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Volumn 43, Issue 6, 2015, Pages e36-

A new recombineering system for Photorhabdus and Xenorhabdus

Author keywords

[No Author keywords available]

Indexed keywords

NONRIBOSOMAL PEPTIDE SYNTHETASE; PHOSPHODIESTERASE I; SPLEEN EXONUCLEASE; TETRACYCLINE; BACTERIAL DNA; BACTERIAL PROTEIN; EXODEOXYRIBONUCLEASE V;

EID: 84936960156     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1336     Document Type: Article
Times cited : (51)

References (53)
  • 1
    • 0031664853 scopus 로고    scopus 로고
    • A new logic for DNA engineering using recombination in Escherichia coli
    • Zhang,Y., Buchholz,F., Muyrers,J.P.P. and Stewart,A.F. (1998) A new logic for DNA engineering using recombination in Escherichia coli. Nat. Genet., 20, 123-128.
    • (1998) Nat. Genet. , vol.20 , pp. 123-128
    • Zhang, Y.1    Buchholz, F.2    Muyrers, J.P.P.3    Stewart, A.F.4
  • 2
    • 0033559118 scopus 로고    scopus 로고
    • Rapid modification of bacterial artificial chromosomes by ET-recombination
    • Muyrers,J.P.P., Zhang,Y., Testa,G. and Stewart,A.F. (1999) Rapid modification of bacterial artificial chromosomes by ET-recombination. Nucleic Acids Res., 27, 1555-1557.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1555-1557
    • Muyrers, J.P.P.1    Zhang, Y.2    Testa, G.3    Stewart, A.F.4
  • 3
    • 0033668496 scopus 로고    scopus 로고
    • DNA cloning by homologous recombination in Escherichia coli
    • Zhang,Y., Muyrers,J.P.P., Testa,G. and Stewart,A.F. (2000) DNA cloning by homologous recombination in Escherichia coli. Nat. Biotechnol., 18, 1314-1317.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1314-1317
    • Zhang, Y.1    Muyrers, J.P.P.2    Testa, G.3    Stewart, A.F.4
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko,K.A. and Wanner,B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A., 97, 6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 0034603783 scopus 로고    scopus 로고
    • PCR-mediated gene replacement in Escherichia coli
    • Murphy,K.C., Campellone,K.G. and Poteete,A.R. (2000) PCR-mediated gene replacement in Escherichia coli. Gene, 246, 321-330.
    • (2000) Gene , vol.246 , pp. 321-330
    • Murphy, K.C.1    Campellone, K.G.2    Poteete, A.R.3
  • 7
    • 0035337803 scopus 로고    scopus 로고
    • Techniques: Recombinogenic engineering-new options for cloning and manipulating DNA
    • Muyrers,J.P.P., Zhang,Y. and Stewart,A.F. (2001) Techniques: recombinogenic engineering-new options for cloning and manipulating DNA. Trends Biochem. Sci., 26, 325-331.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 325-331
    • Muyrers, J.P.P.1    Zhang, Y.2    Stewart, A.F.3
  • 9
    • 0015239451 scopus 로고
    • The role of exonuclease and β protein of phage λ in genetic recombination: II. Substrate specificity and the mode of action of λ exonuclease
    • Carter,D.M. and Radding,C.M. (1971) The role of exonuclease and β protein of phage λ in genetic recombination: II. Substrate specificity and the mode of action of λ exonuclease. J. Biol. Chem., 246, 2502-2512.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2502-2512
    • Carter, D.M.1    Radding, C.M.2
  • 10
    • 0014216084 scopus 로고
    • An exonuclease induced by bacteriophage λ II. Nature of the enzymatic reaction
    • Little,J.W. (1967) An exonuclease induced by bacteriophage λ II. Nature of the enzymatic reaction. J. Biol. Chem., 242, 679-686.
    • (1967) J. Biol. Chem. , vol.242 , pp. 679-686
    • Little, J.W.1
  • 11
    • 0019854161 scopus 로고
    • Beta protein of bacteriophage lambda promotes renaturation of DNA
    • Kmiec,E. and Holloman,W.K. (1981) Beta protein of bacteriophage lambda promotes renaturation of DNA. J. Biol. Chem., 256, 12636-12639.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12636-12639
    • Kmiec, E.1    Holloman, W.K.2
  • 12
    • 0022912797 scopus 로고
    • The homologous recombination system of phage lambda. Pairing activities of beta protein
    • Muniyappa,K. and Radding,C. (1986) The homologous recombination system of phage lambda. Pairing activities of beta protein. J. Biol. Chem., 261, 7472-7478.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7472-7478
    • Muniyappa, K.1    Radding, C.2
  • 13
    • 0032489495 scopus 로고    scopus 로고
    • The beta protein of phage λ binds preferentially to an intermediate in DNA renaturation
    • Karakousis,G., Ye,N., Li,Z., Chiu,S., Reddy,G. and Radding,C. (1998) The beta protein of phage λ binds preferentially to an intermediate in DNA renaturation. J. Mol. Biol., 276, 721-731.
    • (1998) J. Mol. Biol. , vol.276 , pp. 721-731
    • Karakousis, G.1    Ye, N.2    Li, Z.3    Chiu, S.4    Reddy, G.5    Radding, C.6
  • 14
    • 0032489359 scopus 로고    scopus 로고
    • The beta protein of phage λ promotes strand exchange
    • Li,Z., Karakousis,G., Chiu,S., Reddy,G. and Radding,C. (1998) The beta protein of phage λ promotes strand exchange. J. Mol. Biol., 276, 733-744.
    • (1998) J. Mol. Biol. , vol.276 , pp. 733-744
    • Li, Z.1    Karakousis, G.2    Chiu, S.3    Reddy, G.4    Radding, C.5
  • 15
    • 0028233078 scopus 로고
    • Homologous pairing proteins encoded by the Escherichia coli recE and recT genes
    • Kolodner1,R., Hall,S.D. and Luisi-DeLuca,C. (1994) Homologous pairing proteins encoded by the Escherichia coli recE and recT genes. Mol. Biotechnol., 11, 23-30.
    • (1994) Mol. Biotechnol. , vol.11 , pp. 23-30
    • Kolodner, R.1    Hall, S.D.2    Luisi-Deluca, C.3
  • 16
    • 0033624563 scopus 로고    scopus 로고
    • RecE/RecT and Redalpha/Redbeta initiate double-stranded break repair by specifically interacting with their respective partners
    • Muyrers,J.P.P., Zhang,Y., Buchholz,F. and Stewart,A.F. (2000) RecE/RecT and Redalpha/Redbeta initiate double-stranded break repair by specifically interacting with their respective partners. Genes Dev., 14, 1971-1982.
    • (2000) Genes Dev. , vol.14 , pp. 1971-1982
    • Muyrers, J.P.P.1    Zhang, Y.2    Buchholz, F.3    Stewart, A.F.4
  • 17
    • 0019158176 scopus 로고
    • Unwinding and rewinding of DNA by the RecBC enzyme
    • Taylor,A. and Smith,G.R. (1980) Unwinding and rewinding of DNA by the RecBC enzyme. Cell, 22, 447-457.
    • (1980) Cell , vol.22 , pp. 447-457
    • Taylor, A.1    Smith, G.R.2
  • 18
    • 0016754097 scopus 로고
    • The gamma protein specified by bacteriophage gamma. Structure and inhibitory activity for the recBC enzyme of Escherichia coli
    • Karu,A.E., Sakaki,Y., Echols,H. and Linn,S. (1975) The gamma protein specified by bacteriophage gamma. Structure and inhibitory activity for the recBC enzyme of Escherichia coli. J. Biol. Chem., 250, 7377-7387.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7377-7387
    • Karu, A.E.1    Sakaki, Y.2    Echols, H.3    Linn, S.4
  • 19
    • 0025925181 scopus 로고
    • Lambda Gam protein inhibits the helicase and chi-stimulated recombination activities of Escherichia coli RecBCD enzyme
    • Murphy,K.C. (1991) Lambda Gam protein inhibits the helicase and chi-stimulated recombination activities of Escherichia coli RecBCD enzyme. J. Bacteriol., 173, 5808-5821.
    • (1991) J. Bacteriol. , vol.173 , pp. 5808-5821
    • Murphy, K.C.1
  • 20
    • 0015506356 scopus 로고
    • Interaction of the recombination pathways of bacteriophage λ and its host Escherichia coli K12: Effects on exonuclease V activity
    • Unger,R.C. and Clark,A.J. (1972) Interaction of the recombination pathways of bacteriophage λ and its host Escherichia coli K12: effects on exonuclease V activity. J. Mol. Biol., 70, 539-548.
    • (1972) J. Mol. Biol. , vol.70 , pp. 539-548
    • Unger, R.C.1    Clark, A.J.2
  • 21
    • 34447290425 scopus 로고    scopus 로고
    • The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition
    • Court,R., Cook,N., Saikrishnan,K. and Wigley,D. (2007) The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition. J. Mol. Biol., 371, 25-33.
    • (2007) J. Mol. Biol. , vol.371 , pp. 25-33
    • Court, R.1    Cook, N.2    Saikrishnan, K.3    Wigley, D.4
  • 22
    • 34447098490 scopus 로고    scopus 로고
    • The λ Gam protein inhibits RecBCD binding to dsDNA ends
    • Murphy,K.C. (2007) The λ Gam protein inhibits RecBCD binding to dsDNA ends. J. Mol. Biol., 371, 19-24.
    • (2007) J. Mol. Biol. , vol.371 , pp. 19-24
    • Murphy, K.C.1
  • 23
    • 84860778298 scopus 로고    scopus 로고
    • Full-length RecE enhances linear-linear homologous recombination and facilitates direct cloning for bioprospecting
    • Fu,J., Bian,X., Hu,S., Wang,H., Huang,F., Seibert,P.M., Plaza,A., Xia,L., Müller,R., Stewart,A.F. et al. (2012) Full-length RecE enhances linear-linear homologous recombination and facilitates direct cloning for bioprospecting. Nat. Biotechnol., 30, 440-446.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 440-446
    • Fu, J.1    Bian, X.2    Hu, S.3    Wang, H.4    Huang, F.5    Seibert, P.M.6    Plaza, A.7    Xia, L.8    Müller, R.9    Stewart, A.F.10
  • 24
    • 0036843636 scopus 로고    scopus 로고
    • Phenotypes of lexA mutations in Salmonella enterica: Evidence for a lethal lexA null phenotype due to the Fels-2 prophage
    • Bunny,K., Liu,J. and Roth,J. (2002) Phenotypes of lexA mutations in Salmonella enterica: evidence for a lethal lexA null phenotype due to the Fels-2 prophage. J. Bacteriol., 184, 6235-6249.
    • (2002) J. Bacteriol. , vol.184 , pp. 6235-6249
    • Bunny, K.1    Liu, J.2    Roth, J.3
  • 27
    • 33947357684 scopus 로고    scopus 로고
    • Recombineering in Mycobacterium tuberculosis
    • Van Kessel,J.C. and Hatfull,G.F. (2006) Recombineering in Mycobacterium tuberculosis. Nat. Methods, 4, 147-152.
    • (2006) Nat. Methods , vol.4 , pp. 147-152
    • Van Kessel, J.C.1    Hatfull, G.F.2
  • 28
    • 38849190026 scopus 로고    scopus 로고
    • Efficient point mutagenesis in mycobacteria using single-stranded DNA recombineering: Characterization of antimycobacterial drug targets
    • Van Kessel,J.C. and Hatfull,G.F. (2008) Efficient point mutagenesis in mycobacteria using single-stranded DNA recombineering: characterization of antimycobacterial drug targets. Mol. Microbiol., 67, 1094-1107.
    • (2008) Mol. Microbiol. , vol.67 , pp. 1094-1107
    • Van Kessel, J.C.1    Hatfull, G.F.2
  • 30
    • 84857498858 scopus 로고    scopus 로고
    • High efficiency recombineering in lactic acid bacteria
    • van Pijkeren,J.-P. and Britton,R.A. (2012) High efficiency recombineering in lactic acid bacteria. Nucleic Acids Res., 40, e76.
    • (2012) Nucleic Acids Res. , vol.40 , pp. e76
    • Van Pijkeren, J.-P.1    Britton, R.A.2
  • 31
    • 84893425107 scopus 로고    scopus 로고
    • A functional recT gene for recombineering of Clostridium
    • Dong,H., Tao,W., Gong,F., Li,Y. and Zhang,Y. (2013) A functional recT gene for recombineering of Clostridium. J. Biotechnol., 173, 65-67.
    • (2013) J. Biotechnol. , vol.173 , pp. 65-67
    • Dong, H.1    Tao, W.2    Gong, F.3    Li, Y.4    Zhang, Y.5
  • 32
    • 0030774853 scopus 로고    scopus 로고
    • Phylogeny of Photorhabdus and Xenorhabdus species and strains as determined by comparison of partial 16S rRNA gene sequences
    • Liu,J., Berry,R., Poinar,G. and Moldenke,A. (1997) Phylogeny of Photorhabdus and Xenorhabdus species and strains as determined by comparison of partial 16S rRNA gene sequences. Int. J. Syst. Evol. Microbiol., 47, 948-951.
    • (1997) Int. J. Syst. Evol. Microbiol. , vol.47 , pp. 948-951
    • Liu, J.1    Berry, R.2    Poinar, G.3    Moldenke, A.4
  • 34
    • 0028965946 scopus 로고
    • Inability of the polyphasic approach to systematics to determine the relatedness of the genera Xenorhabdus and Photorhabdus
    • Rainey,F.A., Ehlers,R.U. and Stackebrandt,E. (1995) Inability of the polyphasic approach to systematics to determine the relatedness of the genera Xenorhabdus and Photorhabdus. Int. J. Syst. Bacteriol., 45, 379-381.
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 379-381
    • Rainey, F.A.1    Ehlers, R.U.2    Stackebrandt, E.3
  • 35
    • 77955644874 scopus 로고    scopus 로고
    • A metabolic switch is involved in lifestyle decisions in Photorhabdus luminescens
    • Lango,L. and Clarke,D.J. (2010) A metabolic switch is involved in lifestyle decisions in Photorhabdus luminescens. Mol. Microbiol., 77, 1394-1405.
    • (2010) Mol. Microbiol. , vol.77 , pp. 1394-1405
    • Lango, L.1    Clarke, D.J.2
  • 38
    • 84855236038 scopus 로고    scopus 로고
    • Triggering the production of the cryptic blue pigment indigoidine from Photorhabdus luminescens
    • Brachmanna,A.O., Kirchnera,F., Keglera,C., Kinskia,S.C., Schmittb,I. and Bode,H.B. (2012) Triggering the production of the cryptic blue pigment indigoidine from Photorhabdus luminescens. J. Biotechnol., 157, 96-99.
    • (2012) J. Biotechnol. , vol.157 , pp. 96-99
    • Brachmanna, A.O.1    Kirchnera, F.2    Keglera, C.3    Kinskia, S.C.4    Schmittb, I.5    Bode, H.B.6
  • 39
    • 0017519320 scopus 로고
    • Mutations to temperature sensitivity in R plasmid pSC101
    • Hashimoto-Gotoh,T. and Sekiguchi,M. (1977) Mutations to temperature sensitivity in R plasmid pSC101. J. Bacteriol., 131, 405-412.
    • (1977) J. Bacteriol. , vol.131 , pp. 405-412
    • Hashimoto-Gotoh, T.1    Sekiguchi, M.2
  • 40
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman,L.-M., Belin,D., Carson,M. and Beckwith,J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol., 177, 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.3    Beckwith, J.4
  • 41
    • 77955358378 scopus 로고    scopus 로고
    • Chapter eight - A recombineering pipeline to make conditional targeting constructs
    • Fu,J., Teucher,M., Anastassiadis,K., Skarnes,W. and Stewart,A.F. (2010) Chapter eight - a recombineering pipeline to make conditional targeting constructs. Methods Enzymol., 477, 125-144.
    • (2010) Methods Enzymol. , vol.477 , pp. 125-144
    • Fu, J.1    Teucher, M.2    Anastassiadis, K.3    Skarnes, W.4    Stewart, A.F.5
  • 42
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding,J. (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics, 21, 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 45
    • 79959920872 scopus 로고    scopus 로고
    • AntiSMASH: Rapid identification, annotation and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences
    • Medema,M.H., Blin,K., Cimermancic,P., Jager,V.D., Zakrzewski,P., Fischbach,M.A., Weber,T., Takano,E. and Breitling,R. (2011) antiSMASH: rapid identification, annotation and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences. Nucleic Acids Res., 39, W339-W346.
    • (2011) Nucleic Acids Res. , vol.39 , pp. W339-W346
    • Medema, M.H.1    Blin, K.2    Cimermancic, P.3    Jager, V.D.4    Zakrzewski, P.5    Fischbach, M.A.6    Weber, T.7    Takano, E.8    Breitling, R.9
  • 46
    • 40349101854 scopus 로고    scopus 로고
    • Identification and analysis of recombineering functions from Gram-negative and Gram-positive bacteria and their phages
    • Datta,S., Costantino,N. and Zhou,X. (2008) Identification and analysis of recombineering functions from Gram-negative and Gram-positive bacteria and their phages. Proc. Natl. Acad. Sci. U.S.A., 105, 1626-1631.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1626-1631
    • Datta, S.1    Costantino, N.2    Zhou, X.3
  • 47
    • 0030881051 scopus 로고    scopus 로고
    • Toroidal structure of λ-exonuclease
    • Kovall,R. and Matthews,B.W. (1997) Toroidal structure of λ-exonuclease. Science, 277, 1824-1827.
    • (1997) Science , vol.277 , pp. 1824-1827
    • Kovall, R.1    Matthews, B.W.2
  • 48
    • 65149086817 scopus 로고    scopus 로고
    • Crystal structure of E. Coli RecE protein reveals a toroidal tetramer for processing double-stranded DNA breaks
    • Zhang,J., Xing,X., Herr,A.B. and Bell,C.E. (2009) Crystal structure of E. coli RecE protein reveals a toroidal tetramer for processing double-stranded DNA breaks. Structure, 17, 690-702.
    • (2009) Structure , vol.17 , pp. 690-702
    • Zhang, J.1    Xing, X.2    Herr, A.B.3    Bell, C.E.4
  • 49
    • 84856895103 scopus 로고    scopus 로고
    • Determination of the absolute configuration of peptide natural products by using stable isotope labeling and mass spectrometry
    • Bode,H.B., Reimer,D., Fuchs,S.W., Kirchner,F., Dauth,C., Kegler,C., Lorenzen,W., Brachmann,A.O. and Grün,P. (2012) Determination of the absolute configuration of peptide natural products by using stable isotope labeling and mass spectrometry. Chemistry, 18, 2342-2348.
    • (2012) Chemistry , vol.18 , pp. 2342-2348
    • Bode, H.B.1    Reimer, D.2    Fuchs, S.W.3    Kirchner, F.4    Dauth, C.5    Kegler, C.6    Lorenzen, W.7    Brachmann, A.O.8    Grün, P.9
  • 50
    • 84865495161 scopus 로고    scopus 로고
    • Neutral loss fragmentation pattern based screening for arginine-rich natural products in Xenorhabdus and Photorhabdus
    • Fuchs,S.W., Sachs,C.C., Kegler,C., Nollmann,F.I., Karas,M. and Bode,H.B. (2012) Neutral loss fragmentation pattern based screening for arginine-rich natural products in Xenorhabdus and Photorhabdus. Anal. Chem., 84, 6948-6955.
    • (2012) Anal. Chem. , vol.84 , pp. 6948-6955
    • Fuchs, S.W.1    Sachs, C.C.2    Kegler, C.3    Nollmann, F.I.4    Karas, M.5    Bode, H.B.6
  • 51
    • 33845496065 scopus 로고    scopus 로고
    • Metabolic engineering of Pseudomonas putida for methylmalonyl-CoA biosynthesis to enable complex heterologous secondary metabolite formation
    • Gross,F., Ring,M.W., Perlova,O., Fu,J., Schneider,S., Gerth,K., Kuhlmann,S., Stewart,A.F., Zhang,Y. and Muller,R. (2006) Metabolic engineering of Pseudomonas putida for methylmalonyl-CoA biosynthesis to enable complex heterologous secondary metabolite formation. Chem. Biol., 13, 1253-1264.
    • (2006) Chem. Biol. , vol.13 , pp. 1253-1264
    • Gross, F.1    Ring, M.W.2    Perlova, O.3    Fu, J.4    Schneider, S.5    Gerth, K.6    Kuhlmann, S.7    Stewart, A.F.8    Zhang, Y.9    Muller, R.10
  • 52
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin,V.J., Pitera,D.J., Withers,S.T., Newman,J.D. and Keasling,J.D. (2003) Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat. Biotechnol., 21, 796-802.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 796-802
    • Martin, V.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5


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