메뉴 건너뛰기




Volumn 188, Issue 20, 2006, Pages 7062-7071

Regulatory loop between redox sensing of the NADH/NAD+ ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UBIQUINONE;

EID: 33749588803     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00601-06     Document Type: Article
Times cited : (115)

References (28)
  • 1
    • 0015888084 scopus 로고
    • An improved cycling assay for nicotinamide adenine dinucleotide
    • Bernofsky, C., and M. Swan. 1973. An improved cycling assay for nicotinamide adenine dinucleotide. Anal. Biochem. 53:452-458.
    • (1973) Anal. Biochem. , vol.53 , pp. 452-458
    • Bernofsky, C.1    Swan, M.2
  • 2
    • 0141737064 scopus 로고    scopus 로고
    • + redox poise in Streptomyces coelicolor A3(2)
    • + redox poise in Streptomyces coelicolor A3(2). EMBO J. 22:4856-4865.
    • (2003) EMBO J. , vol.22 , pp. 4856-4865
    • Brekasis, D.1    Pagget, M.S.2
  • 3
    • 0015222721 scopus 로고
    • Fate of transforming DNA following uptake by competent Bacillus subtilis. Formation and properties of the donor-recipient complex
    • Dubnau, D., and R. Davidoff-Abelson. 1971. Fate of transforming DNA following uptake by competent Bacillus subtilis. Formation and properties of the donor-recipient complex. J. Mol. Biol. 56:209-221.
    • (1971) J. Mol. Biol. , vol.56 , pp. 209-221
    • Dubnau, D.1    Davidoff-Abelson, R.2
  • 4
    • 1642329678 scopus 로고    scopus 로고
    • Transcriptional activation by Bacillus subtilis ResD: Tandem binding to target elements and phosphorylation-dependent and -independent transcriptional activation
    • Geng, H., S. Nakano, and M. M. Nakano. 2004. Transcriptional activation by Bacillus subtilis ResD: tandem binding to target elements and phosphorylation-dependent and -independent transcriptional activation. J. Bacteriol. 186:2028-2037.
    • (2004) J. Bacteriol. , vol.186 , pp. 2028-2037
    • Geng, H.1    Nakano, S.2    Nakano, M.M.3
  • 5
    • 0001355855 scopus 로고    scopus 로고
    • RNA polymerase and sigma factors
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology Washington, D.C.
    • Helmann, J. D., and C. P. Moran, Jr. 2002. RNA polymerase and sigma factors, p. 289-312. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and its closest relatives: from genes to cells. American Society for Microbiology Washington, D.C.
    • (2002) Bacillus Subtilis and Its Closest Relatives: from Genes to Cells , pp. 289-312
    • Helmann, J.D.1    Moran Jr., C.P.2
  • 6
    • 0036786131 scopus 로고    scopus 로고
    • Mutation in yaaT leads to significant inhibition of phosphorelay during sporulation in Bacillus subtilis
    • Hosoya, S., K. Asai, N. Ogasawara, M. Takeuchi, and T. Sato. 2002. Mutation in yaaT leads to significant inhibition of phosphorelay during sporulation in Bacillus subtilis. J. Bacteriol. 184:5545-5553.
    • (2002) J. Bacteriol. , vol.184 , pp. 5545-5553
    • Hosoya, S.1    Asai, K.2    Ogasawara, N.3    Takeuchi, M.4    Sato, T.5
  • 7
    • 0023032979 scopus 로고
    • Regulation of a promoter that is utilized by minor forms of RNA polymerase holoenzyme in Bacillus subtilis
    • Igo, M. M., and R. Losick. 1986. Regulation of a promoter that is utilized by minor forms of RNA polymerase holoenzyme in Bacillus subtilis. J. Mol. Biol. 191:615-624.
    • (1986) J. Mol. Biol. , vol.191 , pp. 615-624
    • Igo, M.M.1    Losick, R.2
  • 8
    • 3843119815 scopus 로고    scopus 로고
    • spoIVH (ykvV), a requisite cortex formation genes, is expressed in both sporulating compartments of Bacillus subtilis
    • Imamura, D., K. Kobayashi, J. Sekiguchi, N. Ogasawara, M. Takeuchi, and T. Sato. 2004. spoIVH (ykvV), a requisite cortex formation genes, is expressed in both sporulating compartments of Bacillus subtilis. J. Bacteriol. 186:5450-5459.
    • (2004) J. Bacteriol. , vol.186 , pp. 5450-5459
    • Imamura, D.1    Kobayashi, K.2    Sekiguchi, J.3    Ogasawara, N.4    Takeuchi, M.5    Sato, T.6
  • 9
    • 0019513347 scopus 로고
    • Genetic identification and purification of the respiratory NADH dehydrogenase of Escherichia coli
    • Jaworowski, A., H. D. Campbell, M. I. Poulis, and I. G. Young. 1981. Genetic identification and purification of the respiratory NADH dehydrogenase of Escherichia coli. Biochemistry 20:2041-2047.
    • (1981) Biochemistry , vol.20 , pp. 2041-2047
    • Jaworowski, A.1    Campbell, H.D.2    Poulis, M.I.3    Young, I.G.4
  • 10
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., N. Ogasawara, I. Moszer, et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 11
    • 27144540194 scopus 로고    scopus 로고
    • Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis
    • Larsson, J. T., A. Rogstam, and C. von Wachenfeldt. 2005. Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis. Microbiology 151:3323-3335.
    • (2005) Microbiology , vol.151 , pp. 3323-3335
    • Larsson, J.T.1    Rogstam, A.2    Von Wachenfeldt, C.3
  • 12
    • 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
  • 13
    • 0029814919 scopus 로고    scopus 로고
    • Role of NAD in regulating the adhE gene of Escherichia coli
    • Leonardo, M. R., Y. Dailly, and D. P. Clark. 1996. Role of NAD in regulating the adhE gene of Escherichia coli. J. Bacteriol. 178:6013-6018.
    • (1996) J. Bacteriol. , vol.178 , pp. 6013-6018
    • Leonardo, M.R.1    Dailly, Y.2    Clark, D.P.3
  • 14
    • 0033972849 scopus 로고    scopus 로고
    • Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions
    • Marino, M., T. Hoffmann, R. Schmid, H. Mobitz, and D. Jahn. 2000. Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions. Microbiology 146:97-105.
    • (2000) Microbiology , vol.146 , pp. 97-105
    • Marino, M.1    Hoffmann, T.2    Schmid, R.3    Mobitz, H.4    Jahn, D.5
  • 15
    • 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
  • 16
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics, p. 352-355. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 18
    • 0034096905 scopus 로고    scopus 로고
    • Systematic function analysis of Bacillus subtilis genes
    • Ogasawara, N. 2000. Systematic function analysis of Bacillus subtilis genes. Res. Microbiol. 151:129-134.
    • (2000) Res. Microbiol. , vol.151 , pp. 129-134
    • Ogasawara, N.1
  • 19
    • 0002151089 scopus 로고
    • Integrational vectors for genetic manipulation in Bacillus subtilis
    • A. L. Sonenshein, J. H. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington, D.C.
    • Perego, M. 1993. Integrational vectors for genetic manipulation in Bacillus subtilis, p. 615-624. In A. L. Sonenshein, J. H. Hoch, and R. Losick (ed.). Bacillus subtilis and other gram-positive bacteria. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 615-624
    • Perego, M.1
  • 20
    • 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
  • 22
    • 3042857779 scopus 로고    scopus 로고
    • Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon
    • Schau, M., Y. Chen, and F. M. Hulett. 2004. Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon. J. Bacteriol. 186:4585-4595.
    • (2004) J. Bacteriol. , vol.186 , pp. 4585-4595
    • Schau, M.1    Chen, Y.2    Hulett, F.M.3
  • 24
    • 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
  • 25
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH: Ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex 1
    • 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. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex 1. 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
  • 26
    • 0025752593 scopus 로고
    • Bacterial NADH-quinone oxidoreductases
    • Yagi, T. 1991. Bacterial NADH-quinone oxidoreductases. J. Bioenerg. Biomembr. 23:211-215.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 211-215
    • Yagi, T.1
  • 27
    • 0027481581 scopus 로고
    • The bacterial energy-transducing NADH-quinone oxidoreductases
    • Yagi, T. 1993. The bacterial energy-transducing NADH-quinone oxidoreductases. Biochim. Biophys. Acta 1141:1-17.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 1-17
    • Yagi, T.1
  • 28
    • 0033891425 scopus 로고    scopus 로고
    • Global gene expression profiles of Bacillus subtilis grown under anaerobic conditions
    • Ye, R. W., W. Tao, L. Bedzyk, T. Young, M. Chen, and L. Li. 2000. Global gene expression profiles of Bacillus subtilis grown under anaerobic conditions. J. Bacteriol. 182:4458-4465.
    • (2000) J. Bacteriol. , vol.182 , pp. 4458-4465
    • Ye, R.W.1    Tao, W.2    Bedzyk, L.3    Young, T.4    Chen, M.5    Li, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.