메뉴 건너뛰기




Volumn 180, Issue 5, 1998, Pages 1174-1184

Genetic analysis of the nuo locus, which encodes the proton- translocating NADH dehydrogenase in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0031909029     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.5.1174-1184.1998     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 0030023488 scopus 로고    scopus 로고
    • Flagellar assembly in Salmonella typhimurium
    • Aizawa, S. 1996. Flagellar assembly in Salmonella typhimurium. Mol. Microbiol. 19:1-5.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1-5
    • Aizawa, S.1
  • 2
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Anraku, Y., and R. B. Gennis. 1987. The aerobic respiratory chain of Escherichia coli. Trends Biochem. Sci. 12:262-266.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 3
    • 0029065434 scopus 로고
    • Transcriptional control of the nuo operon which encodes the energy conserving NADH dehydrogenase of Salmonella typhimurium
    • Archer, C. D., and T. Elliott. 1995. Transcriptional control of the nuo operon which encodes the energy conserving NADH dehydrogenase of Salmonella typhimurium. J. Bacteriol. 177:2335-2342.
    • (1995) J. Bacteriol. , vol.177 , pp. 2335-2342
    • Archer, C.D.1    Elliott, T.2
  • 4
    • 0027425567 scopus 로고
    • Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation
    • Archer, C. D., X. Wang, and T. Elliott. 1993. Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation. Proc. Natl. Acad. Sci. USA 90:9877-9881.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9877-9881
    • Archer, C.D.1    Wang, X.2    Elliott, T.3
  • 5
    • 2642715163 scopus 로고    scopus 로고
    • Personal communication
    • Barrow, P. A. 1996. Personal communication.
    • (1996)
    • Barrow, P.A.1
  • 8
    • 0029062019 scopus 로고
    • Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-nuoN) of Escherichia coli by electron acceptors, electron donors, and gene regulators
    • Bongaerts, J., S. Zoske, U. Weidner, and G. Unden. 1995. Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-nuoN) of Escherichia coli by electron acceptors, electron donors, and gene regulators. Mol. Microbiol. 16:521-534.
    • (1995) Mol. Microbiol. , vol.16 , pp. 521-534
    • Bongaerts, J.1    Zoske, S.2    Weidner, U.3    Unden, G.4
  • 9
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • in press
    • Braun, M., S. Bungert, and T. Friedrich. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry, in press.
    • Biochemistry
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 10
    • 0027175822 scopus 로고
    • Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli
    • Calhoun, M., and R. B. Gennis. 1993. Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. J. Bacteriol. 175:3013-3019.
    • (1993) J. Bacteriol. , vol.175 , pp. 3013-3019
    • Calhoun, M.1    Gennis, R.B.2
  • 11
    • 0030859256 scopus 로고    scopus 로고
    • Buchnera aphidicola (endosymbiont of aphids) contains nuoC(D) genes that encode subunits of NADH dehydrogenase
    • Clark, M. A., L. Baumann, and P. Baumann. 1997. Buchnera aphidicola (endosymbiont of aphids) contains nuoC(D) genes that encode subunits of NADH dehydrogenase. Curr. Microbiol. 35:122-123.
    • (1997) Curr. Microbiol. , vol.35 , pp. 122-123
    • Clark, M.A.1    Baumann, L.2    Baumann, P.3
  • 12
    • 0029615388 scopus 로고
    • Identification of five Rhodobacter cupsulatus genes encoding the equivalent of ND subunits of the mitochondrial NADH-ubiquinone oxidoreductase
    • Dupuis, A., A. Peinnequin, M. Chevallet, J. Lunardi, E. Darrouzet, B. Pierrard, V. Procaccio, and J. Issartel. 1995. Identification of five Rhodobacter cupsulatus genes encoding the equivalent of ND subunits of the mitochondrial NADH-ubiquinone oxidoreductase. Gene 167:99-104.
    • (1995) Gene , vol.167 , pp. 99-104
    • Dupuis, A.1    Peinnequin, A.2    Chevallet, M.3    Lunardi, J.4    Darrouzet, E.5    Pierrard, B.6    Procaccio, V.7    Issartel, J.8
  • 13
    • 0020641445 scopus 로고
    • A single copy, transducible system for complementation and dominance analysis in Bacillus subtilis
    • Ferrari, E., and J. A. Hoch. 1983. A single copy, transducible system for complementation and dominance analysis in Bacillus subtilis. Mol. Gen. Genet. 189:321-325.
    • (1983) Mol. Gen. Genet. , vol.189 , pp. 321-325
    • Ferrari, E.1    Hoch, J.A.2
  • 14
    • 2642676275 scopus 로고    scopus 로고
    • Personal communication
    • Friedrich, T. 1997. Personal communication.
    • (1997)
    • Friedrich, T.1
  • 15
    • 0024635450 scopus 로고
    • A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa
    • Friedrich, T., G. Hofhaus, W. Ise, U. Nehls, B. Schmitz, and H. Weiss. 1989. A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa. Eur. J. Biochem. 180:173-180.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 173-180
    • Friedrich, T.1    Hofhaus, G.2    Ise, W.3    Nehls, U.4    Schmitz, B.5    Weiss, H.6
  • 18
    • 0000590425 scopus 로고    scopus 로고
    • Origin and evolution of the proton-pumping NADH:ubiquinone oxidoreductase (complex I)
    • H. Baltscheffsky (ed.), VCH Publishers, New York, N.Y
    • Friedrich, T., and H. Weiss. 1996. Origin and evolution of the proton-pumping NADH:ubiquinone oxidoreductase (complex I), p. 205-220. In H. Baltscheffsky (ed.), Origin and evolution of biological energy conversion. VCH Publishers, New York, N.Y.
    • (1996) Origin and Evolution of Biological Energy Conversion , pp. 205-220
    • Friedrich, T.1    Weiss, H.2
  • 19
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules
    • Friedrich, T., and H. Weiss. 1997. Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules. J. Theor. Biol. 187:529-541.
    • (1997) J. Theor. Biol. , vol.187 , pp. 529-541
    • Friedrich, T.1    Weiss, H.2
  • 20
    • 0342273266 scopus 로고
    • Genetics Computer Group, Inc., Madison, Wis
    • Genetics Computer Group, Inc. 1994. Wisconsin Package, version 8.0. Genetics Computer Group, Inc., Madison, Wis.
    • (1994) Wisconsin Package, Version 8.0
  • 21
    • 2642639855 scopus 로고
    • Personal communication
    • Gennis, R. 1995. Personal communication.
    • (1995)
    • Gennis, R.1
  • 22
    • 85081160576 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • in press
    • Guenebaut, V., A. Schlitt, K. Leonard, H. Weiss, and T. Friedrich. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol., in press.
    • J. Mol. Biol.
    • Guenebaut, V.1    Schlitt, A.2    Leonard, K.3    Weiss, H.4    Friedrich, T.5
  • 23
    • 0020807942 scopus 로고
    • Replacement and amplification of bacterial genes with sequences altered in vitro
    • Gutterson, N. I., and D. E. Koshland. 1983. Replacement and amplification of bacterial genes with sequences altered in vitro. Proc. Natl. Acad. Sci. USA 80:4894-4898.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4894-4898
    • Gutterson, N.I.1    Koshland, D.E.2
  • 24
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C. M., M. Aldea, B. K. Washburn, P. Babitzke, and S. R. Kushner. 1989. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171:4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 25
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual, p. 563-566. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual , pp. 563-566
    • Harlow, E.1    Lane, D.2
  • 26
    • 2642614758 scopus 로고
    • Hewlett-Packard Corp., Palo Alto, Calif
    • Hewlett-Packard Corp. 1991. DeskScan II. Hewlett-Packard Corp., Palo Alto, Calif.
    • (1991) DeskScan II
  • 27
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • Hofhaus, G., H. Weiss, and K. Leonard. 1991. Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J. Mol. Biol. 221:1027-1043.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli
    • Leif, H., V. D. Sled, T. Ohnishi, H. Weiss, and T. Friedrich. 1995. Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230:538-548.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 31
    • 0023463947 scopus 로고
    • NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
    • Matsushita, K., T. Ohnishi, and H. R. Kaback. 1987. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26:7732-7737.
    • (1987) Biochemistry , vol.26 , pp. 7732-7737
    • Matsushita, K.1    Ohnishi, T.2    Kaback, H.R.3
  • 33
    • 2642618840 scopus 로고    scopus 로고
    • A Tn5 insertion in the nuo operon of Escherichia coli causes an enhanced dnaN expression and an increase in the frequency of frameshift and deletion mutations
    • abstr. no. PF107. Vereinigung für Allegemeine und Angewandte Mikrobiologie, Hamburg, Germany
    • Meissler, S., R. Langhammer, and A. Quinones. 1997. A Tn5 insertion in the nuo operon of Escherichia coli causes an enhanced dnaN expression and an increase in the frequency of frameshift and deletion mutations, abstr. no. PF107, p. 120. In Abstracts of Sonderausgabe zur Frühjahrstagung of the Vereinigung für Allegemeine und Angewandte Mikrobiologie 1997. Vereinigung für Allegemeine und Angewandte Mikrobiologie, Hamburg, Germany.
    • (1997) Abstracts of Sonderausgabe zur Frühjahrstagung of the Vereinigung für Allegemeine und Angewandte Mikrobiologie 1997 , pp. 120
    • Meissler, S.1    Langhammer, R.2    Quinones, A.3
  • 34
    • 2642649772 scopus 로고
    • Microsoft Corp., Seattle, Wash
    • Microsoft Corp. 1994. PowerPoint, version 4.0. Microsoft Corp., Seattle, Wash.
    • (1994) PowerPoint, Version 4.0
  • 35
  • 36
    • 0028234206 scopus 로고
    • The energetics of bacterial growth: A reassessment
    • Neijessel, O. M., and M. J. Teixeira de Mattos. 1994. The energetics of bacterial growth: a reassessment. Mol. Microbiol. 13:179-182.
    • (1994) Mol. Microbiol. , vol.13 , pp. 179-182
    • Neijessel, O.M.1    Teixeira De Mattos, M.J.2
  • 37
    • 0026805942 scopus 로고
    • Rapid isolation of genomic DNA from gram-negative bacteria
    • Neumann, B., A. Pospiech, and H. U. Schairer. 1992. Rapid isolation of genomic DNA from gram-negative bacteria. Trends Genet. 8:332-333.
    • (1992) Trends Genet. , vol.8 , pp. 332-333
    • Neumann, B.1    Pospiech, A.2    Schairer, H.U.3
  • 38
    • 0021155247 scopus 로고
    • Regulation of the synthesis of ribosomes and ribosomal components
    • Nomura, M., R. Gourse, and G. Baughman. 1984. Regulation of the synthesis of ribosomes and ribosomal components. Annu. Rev. Biochem. 53:75-117.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 39
    • 0022458032 scopus 로고
    • Mutations specifically affecting ligand interaction of the TRG chemosensory transducer
    • Park, C. P., and G. L. Hazelbauer. 1986. Mutations specifically affecting ligand interaction of the TRG chemosensory transducer. J. Bacteriol. 167: 101-109.
    • (1986) J. Bacteriol. , vol.167 , pp. 101-109
    • Park, C.P.1    Hazelbauer, G.L.2
  • 40
    • 0024346011 scopus 로고
    • Mitoskelin: A mitochondrial protein found in cytoskeletal preparations
    • Price, M. G., and R. H. Gomer. 1989. Mitoskelin: a mitochondrial protein found in cytoskeletal preparations. Cell Mot. Cytoskel. 13:274-287.
    • (1989) Cell Mot. Cytoskel. , vol.13 , pp. 274-287
    • Price, M.G.1    Gomer, R.H.2
  • 41
    • 0028095674 scopus 로고
    • Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids
    • Prüß, B. M., J. M. Nelms, C. Park, and A. J. Wolfe. 1994. Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids. J. Bacteriol. 176:2143-2150.
    • (1994) J. Bacteriol. , vol.176 , pp. 2143-2150
    • Prüß, B.M.1    Nelms, J.M.2    Park, C.3    Wolfe, A.J.4
  • 42
    • 0002437098 scopus 로고
    • Amplification of genomic DNA
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), Academic Press, Inc., San Diego, Calif
    • Saiki, R. K. 1990. Amplification of genomic DNA, p. 13-20. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), PCR protocols: a guide to methods and applications. Academic Press, Inc., San Diego, Calif.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 13-20
    • Saiki, R.K.1
  • 44
    • 0026614988 scopus 로고
    • Accumulation of the preassembled membrane arm of NADH:ubiquinone oxidoreductase in mitochondria of manganese-limited grown Neurospora crassa
    • Schmidt, M., T. Friedrich, J. Wallrath, T. Ohnishi, and H. Weiss. 1992. Accumulation of the preassembled membrane arm of NADH:ubiquinone oxidoreductase in mitochondria of manganese-limited grown Neurospora crassa. FEBS Lett. 313:8-11.
    • (1992) FEBS Lett. , vol.313 , pp. 8-11
    • Schmidt, M.1    Friedrich, T.2    Wallrath, J.3    Ohnishi, T.4    Weiss, H.5
  • 46
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53: 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 47
    • 0031047287 scopus 로고    scopus 로고
    • Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications
    • Tran, Q. H., J. Bongaerts, D. Vlad, and G. Unden. 1997. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur. J. Biochem. 244: 155-160.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 155-160
    • Tran, Q.H.1    Bongaerts, J.2    Vlad, D.3    Unden, G.4
  • 48
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden, G., and J. Bongaerts. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta 1320:217-234.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 49
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. 1992. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:253-324.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 50
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli
    • Weidner, U., S. Geier, A. Ptock, T. Friedrich, H. Leif, and H. Weiss. 1993. The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. J. Mol. Biol. 233:109-122.
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 52
    • 0023213791 scopus 로고
    • Reconstitution of signaling in bacterial chemotaxis
    • Wolfe, A. J., M. P. Conley, T. J. Kramer, and H. C. Berg. 1987. Reconstitution of signaling in bacterial chemotaxis. J. Bacteriol. 169:1878-1885.
    • (1987) J. Bacteriol. , vol.169 , pp. 1878-1885
    • Wolfe, A.J.1    Conley, M.P.2    Kramer, T.J.3    Berg, H.C.4
  • 53
    • 0026634739 scopus 로고
    • Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans
    • Xu, X., A. Matsuno-Yagi, and T. Yagi. 1992. Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Arch. Biochem. Biophys. 296: 40-48.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 40-48
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 54
    • 0027477868 scopus 로고
    • DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Xu, X., A. Matsuno-Yagi, and T. Yagi. 1993. DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 32:968-981.
    • (1993) Biochemistry , vol.32 , pp. 968-981
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 55
    • 0031041453 scopus 로고    scopus 로고
    • The protontranslocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8
    • Yano, T., S. S. Chu, V. U. Sled, T. Ohnishi, and T. Yagi. 1997. The protontranslocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. J. Biol. Chem. 272:4201-4211.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4201-4211
    • Yano, T.1    Chu, S.S.2    Sled, V.U.3    Ohnishi, T.4    Yagi, T.5
  • 56
    • 0029864414 scopus 로고    scopus 로고
    • Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano, T., V. D. Sled, T. Ohnishi, and T. Yagi. 1996. Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 271:5907-5913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5907-5913
    • Yano, T.1    Sled, V.D.2    Ohnishi, T.3    Yagi, T.4
  • 57
    • 0029112808 scopus 로고
    • Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the protontranslocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano, T., T. Yagi, V. D. Sled, and T. Ohnishi. 1995. Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the protontranslocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 270:18264-18270.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18264-18270
    • Yano, T.1    Yagi, T.2    Sled, V.D.3    Ohnishi, T.4
  • 58
    • 0017085007 scopus 로고
    • Mutations affecting the reduced nicotinamide adenine dinucleotide dehydrogenase complex of Escherichia coli
    • Young, I. G., and B. J. Wallace. 1976. Mutations affecting the reduced nicotinamide adenine dinucleotide dehydrogenase complex of Escherichia coli. Biochim. Biophys. Acta 449:376-385.
    • (1976) Biochim. Biophys. Acta , vol.449 , pp. 376-385
    • Young, I.G.1    Wallace, B.J.2
  • 59
    • 0001673849 scopus 로고
    • Use of transposons and integrational vectors for mutagenesis and construction of gene fusions in Bacillus species
    • C. R. Harwood and S. M. Cutting (ed.), John Wiley and Sons, West Sussex, England
    • Youngman, P. 1990. Use of transposons and integrational vectors for mutagenesis and construction of gene fusions in Bacillus species, p. 221-257. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. John Wiley and Sons, West Sussex, England.
    • (1990) Molecular Biological Methods for Bacillus , pp. 221-257
    • Youngman, P.1
  • 60
    • 0027216609 scopus 로고
    • Escherichia coli mutants lacking the NADH dehydrogenase I have a competitive disadvantage in stationary phase
    • Zambrano, M. M., and R. Kolter. 1993. Escherichia coli mutants lacking the NADH dehydrogenase I have a competitive disadvantage in stationary phase. J. Bacteriol. 175:5642-5647.
    • (1993) J. Bacteriol. , vol.175 , pp. 5642-5647
    • Zambrano, M.M.1    Kolter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.