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Volumn 150, Issue 4, 2004, Pages 897-910

AstR-AstS, a new two-component signal transduction system, mediates swarming, adaptation to stationary phase and phenotypic variation in Photorhabdus luminescens

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; ASPARAGINE; BACTERIAL PROTEIN; HISTIDINE; PROTEIN ASTR; PROTEIN ASTS; PROTEIN HISTIDINE KINASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 1942505387     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26563-0     Document Type: Article
Times cited : (27)

References (62)
  • 1
    • 0027278037 scopus 로고
    • Flagellin gene transcription in Bordetella bronchiseptica is regulated by the BvgAS virulence control system
    • Akerley, B. J. & Miller, J. F. (1993). Flagellin gene transcription in Bordetella bronchiseptica is regulated by the BvgAS virulence control system. J Bacteriol 175, 3468-3479.
    • (1993) J. Bacteriol. , vol.175 , pp. 3468-3479
    • Akerley, B.J.1    Miller, J.F.2
  • 2
    • 0001304960 scopus 로고
    • Morphological and functional dimorphisms in Xenorhabdus spp., bacteria symbiotically associated with the insect pathogenic nematodes Neoaplectana and Heterorhabditis
    • Akhurst, R. J. (1980). Morphological and functional dimorphisms in Xenorhabdus spp., bacteria symbiotically associated with the insect pathogenic nematodes Neoaplectana and Heterorhabditis. J Gen Microbiol 121, 303-309.
    • (1980) J. Gen. Microbiol. , vol.121 , pp. 303-309
    • Akhurst, R.J.1
  • 3
    • 0024988375 scopus 로고
    • Protein database searches for multiple alignments
    • Altschul, S. F. & Lipman, D. J. (1990). Protein database searches for multiple alignments. Proc Natl Acad Sci U S A 87, 5509-5513.
    • (1990) Proc. Natl. Acad. Sci. U S A , vol.87 , pp. 5509-5513
    • Altschul, S.F.1    Lipman, D.J.2
  • 5
    • 0033818865 scopus 로고    scopus 로고
    • New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis
    • Antoine, R., Alonso, S., Raze, D., Coutte, L., Lesjean, S., Willery, E., Locht, C. & Jacob-Dubuisson, F. (2000). New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis. J Bacteriol 182, 5902-5905.
    • (2000) J. Bacteriol. , vol.182 , pp. 5902-5905
    • Antoine, R.1    Alonso, S.2    Raze, D.3    Coutte, L.4    Lesjean, S.5    Willery, E.6    Locht, C.7    Jacob-Dubuisson, F.8
  • 6
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolomé, B., Jubete, Y., Martinez, E. & de la Cruz, F. (1991). Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102, 75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolomé, B.1    Jubete, Y.2    Martinez, E.3    de la Cruz, F.4
  • 8
    • 0031932852 scopus 로고    scopus 로고
    • Insertional inactivation of genes encoding the crystalline inclusion proteins of Photorhabdus lumincscens results in mutants with pleiotropic phenotypes
    • Bintrim, S. B. & Ensign, J. C. (1998). Insertional inactivation of genes encoding the crystalline inclusion proteins of Photorhabdus lumincscens results in mutants with pleiotropic phenotypes. J Bacteriol 180, 1261-1269.
    • (1998) J. Bacteriol. , vol.180 , pp. 1261-1269
    • Bintrim, S.B.1    Ensign, J.C.2
  • 9
    • 0000452231 scopus 로고
    • Characterization of primary and secondary form of Xenorhabdus luminescens strain HM
    • Bleakley, B. & Nealson, K. H. (1988). Characterization of primary and secondary form of Xenorhabdus luminescens strain HM. FEMS Microbiol Ecol 53, 241-250.
    • (1988) FEMS Microbiol. Ecol. , vol.53 , pp. 241-250
    • Bleakley, B.1    Nealson, K.H.2
  • 10
    • 0036310650 scopus 로고    scopus 로고
    • Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL
    • Bochkareva, E. S., Girshovich, A. S. & Bibi, E. (2002). Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL. Eur J Biochem 269, 3032-3040.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3032-3040
    • Bochkareva, E.S.1    Girshovich, A.S.2    Bibi, E.3
  • 11
    • 0023845377 scopus 로고
    • Biochemical and physiological characterization of colony form variants in Xenorhabdus spp. (Enterobacteriaceae)
    • Boemare, N. E. & Akhurst, R. J. (1988). Biochemical and physiological characterization of colony form variants in Xenorhabdus spp. (Enterobacteriaceae). J Gen Microbiol 134, 751-761.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 751-761
    • Boemare, N.E.1    Akhurst, R.J.2
  • 12
    • 0030920823 scopus 로고    scopus 로고
    • Symbiosis and pathogenicity of nematode-bacterium complexes
    • Boemare, N., Givaudan, A., Brehelin, M. & Laumond, C. (1997). Symbiosis and pathogenicity of nematode-bacterium complexes. Symbiosis 22, 21-45.
    • (1997) Symbiosis , vol.22 , pp. 21-45
    • Boemare, N.1    Givaudan, A.2    Brehelin, M.3    Laumond, C.4
  • 13
    • 0036306492 scopus 로고    scopus 로고
    • The PhlA hemolysin from the entomopathogenic bacterium Photorhabdus luminescens belongs to the two-partner secretion family of hemolysins
    • Brillard, J., Duchaud, E., Boemare, N., Kunst, F. & Givaudan, A. (2002). The PhlA hemolysin from the entomopathogenic bacterium Photorhabdus luminescens belongs to the two-partner secretion family of hemolysins. J Bacteriol 184, 3871-3878.
    • (2002) J. Bacteriol. , vol.184 , pp. 3871-3878
    • Brillard, J.1    Duchaud, E.2    Boemare, N.3    Kunst, F.4    Givaudan, A.5
  • 14
    • 0035149981 scopus 로고    scopus 로고
    • Characterization of spontaneous gacS and gacA regulatory mutants of Pseudomonas fluorescens biocontrol strain CHAO
    • Bull, C. T., Duffy, B., Voisard, C., Defago, G., Keel, C. & Haas, D. (2001). Characterization of spontaneous gacS and gacA regulatory mutants of Pseudomonas fluorescens biocontrol strain CHAO. Antonie Van Leeuwenhoek 79, 327-336.
    • (2001) Antonie van Leeuwenhoek , vol.79 , pp. 327-336
    • Bull, C.T.1    Duffy, B.2    Voisard, C.3    Defago, G.4    Keel, C.5    Haas, D.6
  • 15
    • 0035030870 scopus 로고    scopus 로고
    • A phosphopantetheinyl transferase homolog is essential for Photorhabdus luminescens to support growth and reproduction of the entomopathogenic nematode Heterorhabditis bacteriophora
    • Ciche, T. A., Bintrim, S. B., Horswill, A. R. & Ensign, J. C. (2001). A phosphopantetheinyl transferase homolog is essential for Photorhabdus luminescens to support growth and reproduction of the entomopathogenic nematode Heterorhabditis bacteriophora. J Bacteriol 183, 3117-3126.
    • (2001) J. Bacteriol. , vol.183 , pp. 3117-3126
    • Ciche, T.A.1    Bintrim, S.B.2    Horswill, A.R.3    Ensign, J.C.4
  • 16
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G. & von Heijne, G. (1994). TopPred II: an improved software for membrane protein structure predictions. Comput Appl Biosci 10, 685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    von Heijne, G.2
  • 17
    • 0036324885 scopus 로고    scopus 로고
    • Identification, characterization, and regulation of a cluster of genes involved in carbapenem biosynthesis in Photorhabdus luminescens
    • Derzelle, S., Duchaud, E., Kunst, F., Danchin, A. & Bertin, P. (2002). Identification, characterization, and regulation of a cluster of genes involved in carbapenem biosynthesis in Photorhabdus luminescens. Appl Environ Microbiol 68, 3780-3789.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3780-3789
    • Derzelle, S.1    Duchaud, E.2    Kunst, F.3    Danchin, A.4    Bertin, P.5
  • 18
    • 10744220624 scopus 로고    scopus 로고
    • The Photorhabdus luminescens genome reveals a biotechnological weapon to fight microbes and insect pests
    • & 23 other authors
    • Duchaud, E., Rusniok, C., Frangeul, L. & 23 other authors (2003). The Photorhabdus luminescens genome reveals a biotechnological weapon to fight microbes and insect pests. Nat Biotechnol 21, 1307-1313.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1307-1313
    • Duchaud, E.1    Rusniok, C.2    Frangeul, L.3
  • 19
    • 0000176208 scopus 로고
    • The influence of phase variants of Xenorhabdus spp. and Escherichia coli (Enterobacteriaceae) on the propagation of entomopathogenic nematodes of the genera Steinernema and Heterorhabditis
    • Ehlers, R. D., Stoessel, S. & Whyss, U. (1990). The influence of phase variants of Xenorhabdus spp. and Escherichia coli (Enterobacteriaceae) on the propagation of entomopathogenic nematodes of the genera Steinernema and Heterorhabditis. Rev Nematol 13, 417-424.
    • (1990) Rev. Nematol. , vol.13 , pp. 417-424
    • Ehlers, R.D.1    Stoessel, S.2    Whyss, U.3
  • 20
    • 0037268543 scopus 로고    scopus 로고
    • Photorhabdus: Towards a functional genomic analysis of a symbiont, and pathogen
    • & 7 other authors
    • ffrench-Constant, R., Waterfield, N., Daborn, P. & 7 other authors (2003). Photorhabdus: towards a functional genomic analysis of a symbiont, and pathogen. FEMS Microbiol Rev 26, 433-456.
    • (2003) FEMS Microbiol. Rev. , vol.26 , pp. 433-456
    • ffrench-Constant, R.1    Waterfield, N.2    Daborn, P.3
  • 21
    • 0032754137 scopus 로고    scopus 로고
    • Polyphasic classification of the genus Photorhabdus and proposal of new taxa: P. luminescens subsp. luminescens subsp. nov., P. luminescens subsp. akhurstii subsp. nov., P. luminescens subsp. laumondii subsp. nov., P. temperata sp. nov., P. temperata subsp. temperata subsp. nov. and P. asymbiotica sp. nov
    • Fischer-Le Saux, M., Viallard, V., Brunel, B., Normand, P. & Boemare, N. E. (1999). Polyphasic classification of the genus Photorhabdus and proposal of new taxa: P. luminescens subsp. luminescens subsp. nov., P. luminescens subsp. akhurstii subsp. nov., P. luminescens subsp. laumondii subsp. nov., P. temperata sp. nov., P. temperata subsp. temperata subsp. nov. and P. asymbiotica sp. nov. Int J Syst Bacteriol 49, 1645-1656.
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 1645-1656
    • Fischer-Le Saux, M.1    Viallard, V.2    Brunel, B.3    Normand, P.4    Boemare, N.E.5
  • 22
    • 0003086394 scopus 로고    scopus 로고
    • Bacteria-nematode symbiosis
    • Edited by R. Gaugler. London: CAB International
    • Forst, S. & Clarke, D. (2002). Bacteria-nematode symbiosis. In Entomopathogenic Nematology, pp. 57-77. Edited by R. Gaugler. London: CAB International.
    • (2002) Entomopathogenic Nematology , pp. 57-77
    • Forst, S.1    Clarke, D.2
  • 24
    • 0028971666 scopus 로고
    • bvg repression of alcaligin synthesis in Bordetella bronchiseptica is associated with phylogenetic lineage
    • Giardina, P. C., Foster, L.-A., Musser, J. M., Akerley, B. J., Miller, J. F. & Dyer, D. W. (1995). bvg repression of alcaligin synthesis in Bordetella bronchiseptica is associated with phylogenetic lineage. J Bacteriol 177, 6058-6063.
    • (1995) J. Bacteriol. , vol.177 , pp. 6058-6063
    • Giardina, P.C.1    Foster, L.-A.2    Musser, J.M.3    Akerley, B.J.4    Miller, J.F.5    Dyer, D.W.6
  • 25
    • 0033989675 scopus 로고    scopus 로고
    • flhDC, the flagellar master operon of Xenorhabdus nematophilus: Requirement for motility, lipolysis, extracellular hemolysis, and full virulence in insects
    • Givaudan, A. & Lanois, A. (2000). flhDC, the flagellar master operon of Xenorhabdus nematophilus: requirement for motility, lipolysis, extracellular hemolysis, and full virulence in insects. J Bacteriol 182, 107-115.
    • (2000) J. Bacteriol. , vol.182 , pp. 107-115
    • Givaudan, A.1    Lanois, A.2
  • 26
    • 84988122211 scopus 로고
    • Elimination of point streaking on silver-stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer
    • Gorg, A., Postel, W., Weser, J., Günther, S., Strahler, J. R., Hanash, S. M. & Somerlot, L. (1987). Elimination of point streaking on silver-stained two-dimensional gels by addition of iodoacetamide to the equilibration buffer. Electrophoresis 8, 122-124.
    • (1987) Electrophoresis , vol.8 , pp. 122-124
    • Gorg, A.1    Postel, W.2    Weser, J.3    Günther, S.4    Strahler, J.R.5    Hanash, S.M.6    Somerlot, L.7
  • 27
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized PH gradients
    • Gorg, A., Postel, W. & Gunther, S. (1988). The current state of two-dimensional electrophoresis with immobilized PH gradients. Electrophoresis 9, 531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 28
    • 0041172666 scopus 로고    scopus 로고
    • Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions
    • Gothel, S. F., Scholz, C., Schmid, F. X. & Marahiel, M. A. (1998). Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. Biochemistry 37, 13392-13399.
    • (1998) Biochemistry , vol.37 , pp. 13392-13399
    • Gothel, S.F.1    Scholz, C.2    Schmid, F.X.3    Marahiel, M.A.4
  • 29
    • 0035783391 scopus 로고    scopus 로고
    • Review: A structural view of the GroE chaperone cycle
    • Grallert, H. & Buchner, J. (2001). Review: a structural view of the GroE chaperone cycle. J Struct Biol 135, 95-103.
    • (2001) J. Struct. Biol. , vol.135 , pp. 95-103
    • Grallert, H.1    Buchner, J.2
  • 30
    • 0036192462 scopus 로고    scopus 로고
    • The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage
    • Gustavsson, N., Diez, A. A. & Nyström, T. (2002). The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage. Mol Microbiol 43, 107-117.
    • (2002) Mol. Microbiol. , vol.43 , pp. 107-117
    • Gustavsson, N.1    Diez, A.A.2    Nyström, T.3
  • 31
    • 0033000503 scopus 로고    scopus 로고
    • Expression of bvgAS of Bordetella pertussis represses flagellar biosynthesis of Escherichia coli
    • Han, Y. W., Uhl, M. A., Han, S. J. & Shi, W. (1999). Expression of bvgAS of Bordetella pertussis represses flagellar biosynthesis of Escherichia coli. Arch Microbiol 171, 127-130.
    • (1999) Arch. Microbiol. , vol.171 , pp. 127-130
    • Han, Y.W.1    Uhl, M.A.2    Han, S.J.3    Shi, W.4
  • 32
    • 0035088468 scopus 로고    scopus 로고
    • Transcriptional regulation of the moe (molybdate metabolism) operon of Escherichia coli
    • Hasona, A., Self, W. T. & Shanmugam, K. T. (2001). Transcriptional regulation of the moe (molybdate metabolism) operon of Escherichia coli. Arch Microbiol 175, 178-188.
    • (2001) Arch. Microbiol. , vol.175 , pp. 178-188
    • Hasona, A.1    Self, W.T.2    Shanmugam, K.T.3
  • 33
    • 0034193079 scopus 로고    scopus 로고
    • Common molecular mechanisms of symbiosis and pathogenesis
    • Hentschel, U., Steinert, M. & Hacker, J. (2000). Common molecular mechanisms of symbiosis and pathogenesis. Trends Microbiol 8, 226-231.
    • (2000) Trends Microbiol. , vol.8 , pp. 226-231
    • Hentschel, U.1    Steinert, M.2    Hacker, J.3
  • 34
    • 0028269731 scopus 로고
    • The amino acid sequences of human and pig L-arginine: Glycine amidinotransferase
    • Humm, A., Huber, R. & Mann, K. (1994). The amino acid sequences of human and pig L-arginine:glycine amidinotransferase. FEBS Lett 339, 101-107.
    • (1994) FEBS Lett. , vol.339 , pp. 101-107
    • Humm, A.1    Huber, R.2    Mann, K.3
  • 35
    • 0342859838 scopus 로고
    • Investigations into the pathogenic mechanisms of the bacterium-nematode complex
    • Hurlbert, R. E. (1994). Investigations into the pathogenic mechanisms of the bacterium-nematode complex. ASM News 60, 473-478.
    • (1994) ASM News , vol.60 , pp. 473-478
    • Hurlbert, R.E.1
  • 36
    • 0037340032 scopus 로고    scopus 로고
    • A hexA homologue from Photorhabdus regulates pathogenicity, symbiosis and phenotypic variation
    • Joyce, S. A. & Clarke, D. J. (2003). A hexA homologue from Photorhabdus regulates pathogenicity, symbiosis and phenotypic variation. Mol Microbiol 47, 1445-1457.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1445-1457
    • Joyce, S.A.1    Clarke, D.J.2
  • 37
    • 0035084793 scopus 로고    scopus 로고
    • Differential regulation of Bvg-activated virulence factors plays a role in Bordetella pertussis pathogenicity
    • Kinnear, S. M., Marques, R. R. & Carbonetti, N. H. (2001). Differential regulation of Bvg-activated virulence factors plays a role in Bordetella pertussis pathogenicity. Infect Immun 69, 1983-1993.
    • (2001) Infect. Immun. , vol.69 , pp. 1983-1993
    • Kinnear, S.M.1    Marques, R.R.2    Carbonetti, N.H.3
  • 38
    • 0028839451 scopus 로고
    • Influence of osmolarity on phase shift in Photorhabdus luminescens
    • Krasomil-Osterfeld, K. C. (1995). Influence of osmolarity on phase shift in Photorhabdus luminescens. Appl Environ Microbiol 61, 3748-3749.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3748-3749
    • Krasomil-Osterfeld, K.C.1
  • 39
    • 0035151048 scopus 로고    scopus 로고
    • Bordetella pertussis, molecular pathogenesis under multiple aspects
    • Locht, C., Antoine, R. & Jacob-Dubuisson, F. (2001). Bordetella pertussis, molecular pathogenesis under multiple aspects. Curr Opinion Microbiol 4, 82-89.
    • (2001) Curr. Opinion Microbiol. , vol.4 , pp. 82-89
    • Locht, C.1    Antoine, R.2    Jacob-Dubuisson, F.3
  • 42
    • 0028225734 scopus 로고
    • Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest
    • Nyström, T. & Neidhardt, F. C. (1994). Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Mol Microbiol 11, 537-544.
    • (1994) Mol. Microbiol. , vol.11 , pp. 537-544
    • Nyström, T.1    Neidhardt, F.C.2
  • 43
    • 0036098108 scopus 로고    scopus 로고
    • The ner gene of Photorhabdus: Effects on primary-form-specific phenotypes and outer membrane protein composition
    • O'Neill, K. H., Roche, D. M., Clarke, D. J. & Dowds, B. C. (2002). The ner gene of Photorhabdus: effects on primary-form-specific phenotypes and outer membrane protein composition. J Bacteriol 184, 3096-3105.
    • (2002) J. Bacteriol. , vol.184 , pp. 3096-3105
    • O'Neill, K.H.1    Roche, D.M.2    Clarke, D.J.3    Dowds, B.C.4
  • 44
    • 0018887163 scopus 로고
    • Identification of antigen 19/27 as dihydrolipoyl dehydrogenase and its probable involvement in ubiquinone-mediated NADH-dependent transport phenomena in membrane vesicles of Escherichia coli
    • Owen, P., Kaback, H. R. & Graeme-Cook, K. A. (1980). Identification of antigen 19/27 as dihydrolipoyl dehydrogenase and its probable involvement in ubiquinone-mediated NADH-dependent transport phenomena in membrane vesicles of Escherichia coli. FEMS Microbiol Lett 7, 345-348.
    • (1980) FEMS Microbiol. Lett. , vol.7 , pp. 345-348
    • Owen, P.1    Kaback, H.R.2    Graeme-Cook, K.A.3
  • 45
    • 0035313419 scopus 로고    scopus 로고
    • FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions
    • Prüß, B. M., Liu, X., Hendrickson, W. & Matsumura, P. (2001). FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions. FEMS Microbiol Lett 197, 91-97.
    • (2001) FEMS Microbiol. Lett. , vol.197 , pp. 91-97
    • Prüß, B.M.1    Liu, X.2    Hendrickson, W.3    Matsumura, P.4
  • 46
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt, J. & Hynes, M. F. (1993). Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127, 15-21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 47
    • 0028603364 scopus 로고
    • Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension
    • Rabilloud, T., Valette, C. & Lawrence, J. J. (1994). Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension. Electrophoresis 15, 1552-1558.
    • (1994) Electrophoresis , vol.15 , pp. 1552-1558
    • Rabilloud, T.1    Valette, C.2    Lawrence, J.J.3
  • 50
    • 0036189505 scopus 로고    scopus 로고
    • Phenotypic selection and phase variation occur during alfalfa root colonization by Pseudomonas fluorescens F113
    • Sanchez-Contreras, M., Martin, M., Villacieros, M., O'Gara, F., Bonilla, I. & Rivilla, R. (2002). Phenotypic selection and phase variation occur during alfalfa root colonization by Pseudomonas fluorescens F113. J Bacteriol 184, 1587-1596.
    • (2002) J. Bacteriol. , vol.184 , pp. 1587-1596
    • Sanchez-Contreras, M.1    Martin, M.2    Villacieros, M.3    O'Gara, F.4    Bonilla, I.5    Rivilla, R.6
  • 51
    • 0034876645 scopus 로고    scopus 로고
    • Lipoamide dehydrogenase from Corynebacterium glutamicum: Molecular and physiological analysis of the lpd gene and characterization of the enzyme
    • Schwinde, J. W., Hertz, P. F., Sahm, H., Eikmanns, B. J. & Guyonvarch, A. (2001). Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme. Microbiology 147, 2223-2231.
    • (2001) Microbiology , vol.147 , pp. 2223-2231
    • Schwinde, J.W.1    Hertz, P.F.2    Sahm, H.3    Eikmanns, B.J.4    Guyonvarch, A.5
  • 52
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. (1996). Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 53
    • 0021205685 scopus 로고
    • High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-Mob transposon
    • Simon, R. (1984). High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-Mob transposon. Mol Gen Genet 196, 413-420.
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 413-420
    • Simon, R.1
  • 54
    • 0028120705 scopus 로고
    • Phase variation in Xenorhabdus nematophilus and Photorhabdus luminescens: Differences in respiratory activity and membrane energization
    • Smigielski, A., Auhkurst, R. J. & Boemare, N. E. (1994). Phase variation in Xenorhabdus nematophilus and Photorhabdus luminescens: differences in respiratory activity and membrane energization. Appl Environ Microbiol 60, 120-125.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 120-125
    • Smigielski, A.1    Auhkurst, R.J.2    Boemare, N.E.3
  • 55
    • 0033823229 scopus 로고    scopus 로고
    • Prokaryotic carbonic anhydrases
    • Smith, K. S. & Ferry, J. G. (2000). Prokaryotic carbonic anhydrases. FEMS Microbiol Rev 24, 335-366.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 335-366
    • Smith, K.S.1    Ferry, J.G.2
  • 56
    • 0021066245 scopus 로고
    • 2-Oxoacid dehydrogenase complexes of Escherichia coli: Cellular amounts and patterns of synthesis
    • Smith, M. W. & Neidhardt, F. C. (1983). 2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis. J Bacteriol 156, 81-88.
    • (1983) J. Bacteriol. , vol.156 , pp. 81-88
    • Smith, M.W.1    Neidhardt, F.C.2
  • 58
    • 0028977970 scopus 로고
    • Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH
    • Thorn, J. M., Barton, J. D., Dixon, N. E., Ollis, D. L. & Edwards, K. J. (1995). Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J Mol Biol 249, 785-799.
    • (1995) J. Mol. Biol. , vol.249 , pp. 785-799
    • Thorn, J.M.1    Barton, J.D.2    Dixon, N.E.3    Ollis, D.L.4    Edwards, K.J.5
  • 59
    • 0029871035 scopus 로고    scopus 로고
    • Integration of multiple domains in a two-component sensor protein: The Bordetella pertussis BvgAS phosphorelay
    • Uhl, A. M. & Miller, J. F. (1996). Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay. EMBO J 15, 1028-1036.
    • (1996) EMBO J. , vol.15 , pp. 1028-1036
    • Uhl, A.M.1    Miller, J.F.2
  • 60
    • 0030614441 scopus 로고    scopus 로고
    • Hymenolepis diminuta: Mitochondrial NADH/NAD transhydrogenation and the lipoamide dehydrogenase system
    • Walker, D. J., Burkhart, W. & Fioravanti, C. F. (1997). Hymenolepis diminuta: mitochondrial NADH/NAD transhydrogenation and the lipoamide dehydrogenase system. Exp Parasitol 85, 158-167.
    • (1997) Exp. Parasitol. , vol.85 , pp. 158-167
    • Walker, D.J.1    Burkhart, W.2    Fioravanti, C.F.3
  • 61
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A. & Bray, R. C. (1991). Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim Biophys Acta 1057, 157-185.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7
  • 62
    • 0034697253 scopus 로고    scopus 로고
    • Enhanced sensitivity of Streptomyces seoulensis to menadione by superfluous lipoamide dehydrogenase
    • Youn, H. & Kang, S. O. (2000). Enhanced sensitivity of Streptomyces seoulensis to menadione by superfluous lipoamide dehydrogenase. FEBS Lett 472, 57-61.
    • (2000) FEBS Lett. , vol.472 , pp. 57-61
    • Youn, H.1    Kang, S.O.2


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