메뉴 건너뛰기




Volumn 186, Issue 24, 2004, Pages 8424-8432

Terminal oxidases are essential to bypass the requirement for ResD for full Pho induction in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; CYTOCHROME BD; OXIDOREDUCTASE; PHOSPHATE; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 10044250045     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.24.8424-8432.2004     Document Type: Article
Times cited : (24)

References (56)
  • 1
    • 0033895238 scopus 로고    scopus 로고
    • Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis
    • Antelmann, H., C. Scharf, and M. Hecker. 2000. Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis. J. Bacteriol. 182:4478-4490.
    • (2000) J. Bacteriol. , vol.182 , pp. 4478-4490
    • Antelmann, H.1    Scharf, C.2    Hecker, M.3
  • 2
    • 0032900982 scopus 로고    scopus 로고
    • Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein
    • Bengtsson, J., H. Tjalsma, C. Rivolta, and L. Hederstedt. 1999. Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein. J. Bacteriol. 181:685-688.
    • (1999) J. Bacteriol. , vol.181 , pp. 685-688
    • Bengtsson, J.1    Tjalsma, H.2    Rivolta, C.3    Hederstedt, L.4
  • 3
    • 0031739510 scopus 로고    scopus 로고
    • Pho signal transduction network reveals direct transcriptional regulation of one two-component system by another two-component regulator: Bacillus subtilis PhoP directly regulates production of ResD
    • Birkey, S. M., W. Liu, X. Zhang, M. F. Duggan, and F. M. Hulett. 1998. Pho signal transduction network reveals direct transcriptional regulation of one two-component system by another two-component regulator: Bacillus subtilis PhoP directly regulates production of ResD. Mol. Microbiol. 30:943-953.
    • (1998) Mol. Microbiol. , vol.30 , pp. 943-953
    • Birkey, S.M.1    Liu, W.2    Zhang, X.3    Duggan, M.F.4    Hulett, F.M.5
  • 4
    • 0017154836 scopus 로고
    • Reconstitution of reduced nicotinamide adenine dinucleotide oxidase activity with menadione in membrane vesicles from the menaquinone-deficient Bacillus subtilis aroD. Relation between electron transfer and active transport
    • Bisschop, A., and W. N. Konings. 1976. Reconstitution of reduced nicotinamide adenine dinucleotide oxidase activity with menadione in membrane vesicles from the menaquinone-deficient Bacillus subtilis aroD. Relation between electron transfer and active transport. Eur. J. Biochem. 67:357-365.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 357-365
    • Bisschop, A.1    Konings, W.N.2
  • 5
    • 0036375536 scopus 로고    scopus 로고
    • The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier
    • Bock, A., and R. Gross. 2002. The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier. Eur. J. Biochem. 269:3479-3484.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3479-3484
    • Bock, A.1    Gross, R.2
  • 6
    • 0025964291 scopus 로고
    • Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay
    • Burbulys, D., K. A. Trach, and J. A. Hoch. 1991. Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay. Cell 64:545-552.
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 7
    • 0025783281 scopus 로고
    • Separate promoters direct expression of phoAIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation
    • Chesnut, R. S., C. Bookstein, and F. M. Hulett. 1991. Separate promoters direct expression of phoAIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation. Mol. Microbiol. 5:2181-2190.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2181-2190
    • Chesnut, R.S.1    Bookstein, C.2    Hulett, F.M.3
  • 8
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications
    • Collins, M. D., and D. Jones. 1981. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications. Microbiol. Rev. 45:316-354.
    • (1981) Microbiol. Rev. , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 9
    • 0002301028 scopus 로고
    • Genetic analysis
    • C. R. Harwood and S. M. Cutting (ed.). John Wiley & Sons, Inc., New York, N.Y.
    • Cutting, S. M., and P. B. Vander Horn. 1990. Genetic analysis, p. 24-74. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. John Wiley & Sons, Inc., New York, N.Y.
    • (1990) Molecular Biological Methods for Bacillus , pp. 24-74
    • Cutting, S.M.1    Vander Horn, P.B.2
  • 10
    • 0023643136 scopus 로고
    • Spectral and potentiometric analysis of cytochromes from Bacillus subtilis
    • de Vrij, W., B. van den Burg, and W. N. Konings. 1987. Spectral and potentiometric analysis of cytochromes from Bacillus subtilis. Eur. J. Biochem. 166:589-595.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 589-595
    • De Vrij, W.1    Van Den Burg, B.2    Konings, W.N.3
  • 11
    • 0029849654 scopus 로고    scopus 로고
    • A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD
    • Eder, S., L. Shi, K. Jensen, K. Yamane, and F. M. Hulett. 1996. A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD. Microbiology 142:2041-2047.
    • (1996) Microbiology , vol.142 , pp. 2041-2047
    • Eder, S.1    Shi, L.2    Jensen, K.3    Yamane, K.4    Hulett, F.M.5
  • 12
    • 0022530657 scopus 로고
    • Effect of stage 0 sporulation mutations on subtilisin expression
    • Ferrari, E., S. M. Howard, and J. A. Hoch. 1986. Effect of stage 0 sporulation mutations on subtilisin expression. J. Bacteriol. 166:173-179.
    • (1986) J. Bacteriol. , vol.166 , pp. 173-179
    • Ferrari, E.1    Howard, S.M.2    Hoch, J.A.3
  • 13
    • 0035933597 scopus 로고    scopus 로고
    • Quinones as the redox signal for the Arc two-component system of bacteria
    • Georgellis, D., O. Kwon, and E. C. Lin. 2001. Quinones as the redox signal for the Arc two-component system of bacteria. Science 292:2314-2316.
    • (2001) Science , vol.292 , pp. 2314-2316
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.3
  • 14
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A. M., K. Shazand, N. Frandsen, and P. Stragier. 1995. Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167:335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 15
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coli
    • D. M. Glover (ed.). IRL Press, Washington, D.C.
    • Hanahan, D. 1985. Techniques for transformation of E. coli, p. 109-135. In D. M. Glover (ed.), DNA cloning II: a practical approach. IRL Press, Washington, D.C.
    • (1985) DNA Cloning II: A Practical Approach , pp. 109-135
    • Hanahan, D.1
  • 16
    • 0025285066 scopus 로고
    • Inducible expression of regulatory genes in Bacillus subtilis
    • Henner, D. J. 1990. Inducible expression of regulatory genes in Bacillus subtilis. Methods Enzymol. 185:223-228.
    • (1990) Methods Enzymol. , vol.185 , pp. 223-228
    • Henner, D.J.1
  • 17
    • 0032844453 scopus 로고    scopus 로고
    • Transcriptional control of Bacillus subtilis hemN and hemZ
    • Homuth, G., A. Rompf, W. Schumann, and D. Jahn. 1999. Transcriptional control of Bacillus subtilis hemN and hemZ. J. Bacteriol. 181:5922-5929.
    • (1999) J. Bacteriol. , vol.181 , pp. 5922-5929
    • Homuth, G.1    Rompf, A.2    Schumann, W.3    Jahn, D.4
  • 18
    • 0025136856 scopus 로고
    • Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis
    • Hulett, F. M., C. Bookstein, and K. Jensen. 1990. Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis. J. Bacteriol. 172:735-740.
    • (1990) J. Bacteriol. , vol.172 , pp. 735-740
    • Hulett, F.M.1    Bookstein, C.2    Jensen, K.3
  • 19
    • 0025977645 scopus 로고
    • Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure
    • Hulett, F. M., E. E. Kim, C. Bookstein, N. V. Kapp, C. W. Edwards, and H. W. Wyckoff. 1991. Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure. J. Biol. Chem. 266:1077-1084.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1077-1084
    • Hulett, F.M.1    Kim, E.E.2    Bookstein, C.3    Kapp, N.V.4    Edwards, C.W.5    Wyckoff, H.W.6
  • 20
    • 0028203258 scopus 로고
    • Sequential action of two-component genetic switches regulates the Pho regulon in Bacillus subtilis
    • Hulett, F. M., J. Lee, L. Shi, G. Sun, R. Chesnut, E. Sharkova, M. F. Duggan, and N. Kapp. 1994. Sequential action of two-component genetic switches regulates the Pho regulon in Bacillus subtilis. J. Bacteriol. 176:1348-1358.
    • (1994) J. Bacteriol. , vol.176 , pp. 1348-1358
    • Hulett, F.M.1    Lee, J.2    Shi, L.3    Sun, G.4    Chesnut, R.5    Sharkova, E.6    Duggan, M.F.7    Kapp, N.8
  • 21
    • 0025144171 scopus 로고
    • Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study utilizing deletions and lac fusions of cyo and cyd
    • Iuchi, S., V. Chepuri, H. A. Fu, R. B. Gennis, and E. C. Lin. 1990. Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd. J. Bacteriol. 172:6020-6025.
    • (1990) J. Bacteriol. , vol.172 , pp. 6020-6025
    • Iuchi, S.1    Chepuri, V.2    Fu, H.A.3    Gennis, R.B.4    Lin, E.C.5
  • 22
    • 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 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0026453363 scopus 로고
    • Nucleotide sequence of the phoP gene encoding PhoP, the response regulator of the phosphate regulon of Bacillus subtilis
    • Lee, J. W., and F. M. Hulett. 1992. Nucleotide sequence of the phoP gene encoding PhoP, the response regulator of the phosphate regulon of Bacillus subtilis. Nucleic Acids Res. 20:5848.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5848
    • Lee, J.W.1    Hulett, F.M.2
  • 24
    • 0025647235 scopus 로고
    • Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis
    • Lemma, E., G. Unden, and A. Kroger. 1990. Menaquinone is an obligatory component of the chain catalyzing succinate respiration in Bacillus subtilis. Arch. Microbiol. 155:62-67.
    • (1990) Arch. Microbiol. , vol.155 , pp. 62-67
    • Lemma, E.1    Unden, G.2    Kroger, A.3
  • 26
    • 0031912067 scopus 로고    scopus 로고
    • Analysis of Bacillus subtilis tagAB and tagDEF expression during phosphate starvation identifies a repressor role for PhoP-P
    • Liu, W., S. Eder, and F. M. Hulett. 1998. Analysis of Bacillus subtilis tagAB and tagDEF expression during phosphate starvation identifies a repressor role for PhoP-P. J. Bacteriol. 180:753-758.
    • (1998) J. Bacteriol. , vol.180 , pp. 753-758
    • Liu, W.1    Eder, S.2    Hulett, F.M.3
  • 27
    • 2642705037 scopus 로고    scopus 로고
    • Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site
    • Liu, W., and F. M. Hulett. 1998. Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site. Microbiology 144:1443-1450.
    • (1998) Microbiology , vol.144 , pp. 1443-1450
    • Liu, W.1    Hulett, F.M.2
  • 28
    • 0031726032 scopus 로고    scopus 로고
    • Catabolite regulation of the Bacillus subtilis ctaBCDEF gene cluster
    • Liu, X., and H. W. Taber. 1998. Catabolite regulation of the Bacillus subtilis ctaBCDEF gene cluster. J. Bacteriol. 180:6154-6163.
    • (1998) J. Bacteriol. , vol.180 , pp. 6154-6163
    • Liu, X.1    Taber, H.W.2
  • 30
    • 0024729626 scopus 로고
    • Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis
    • Mueller, J. P., and H. W. Taber. 1989. Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis. J. Bacteriol. 171:4967-4978.
    • (1989) J. Bacteriol. , vol.171 , pp. 4967-4978
    • Mueller, J.P.1    Taber, H.W.2
  • 31
    • 0034087235 scopus 로고    scopus 로고
    • Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis
    • Nakano, M. M., G. Zheng, and P. Zuber. 2000. Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis. J. Bacteriol. 182:3274-3277.
    • (2000) J. Bacteriol. , vol.182 , pp. 3274-3277
    • Nakano, M.M.1    Zheng, G.2    Zuber, P.3
  • 32
    • 0033812771 scopus 로고    scopus 로고
    • Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis
    • Nakano, M. M., Y. Zhu, M. Lacelle, X. Zhang, and F. M. Hulett. 2000. Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis. Mol. Microbiol. 37:1198-1207.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1198-1207
    • Nakano, M.M.1    Zhu, Y.2    Lacelle, M.3    Zhang, X.4    Hulett, F.M.5
  • 33
    • 85102610294 scopus 로고
    • Phosphate nutrition of plants-a general treatise
    • E. Khasswenh (ed.). American Society of Agronomy, Madison, Wis.
    • Ozanne, P. G. 1980. Phosphate nutrition of plants-a general treatise, p. 559-585. In E. Khasswenh (ed.), The role of phosphorus in agriculture. American Society of Agronomy, Madison, Wis.
    • (1980) The Role of Phosphorus in Agriculture , pp. 559-585
    • Ozanne, P.G.1
  • 35
    • 0035030871 scopus 로고    scopus 로고
    • Two ResD-controlled promoters regulate ctaA expression in Bacillus subtilis
    • Paul, S., X. Zhang, and F. M. Hulett. 2001. Two ResD-controlled promoters regulate ctaA expression in Bacillus subtilis. J. Bacteriol. 183:3237-3246.
    • (2001) J. Bacteriol. , vol.183 , pp. 3237-3246
    • Paul, S.1    Zhang, X.2    Hulett, F.M.3
  • 36
    • 0035091230 scopus 로고    scopus 로고
    • + antiporter, influences expression of the phoPR operon and production of alkaline phosphatases
    • + antiporter, influences expression of the phoPR operon and production of alkaline phosphatases. J. Bacteriol. 183:2505-2515.
    • (2001) J. Bacteriol. , vol.183 , pp. 2505-2515
    • Pragai, Z.1    Eschevins, C.2    Bron, S.3    Harwood, C.R.4
  • 37
    • 0030895003 scopus 로고    scopus 로고
    • The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon
    • Qi, Y., Y. Kobayashi, and F. M. Hulett. 1997. The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon. J. Bacteriol. 179:2534-2539.
    • (1997) J. Bacteriol. , vol.179 , pp. 2534-2539
    • Qi, Y.1    Kobayashi, Y.2    Hulett, F.M.3
  • 38
    • 0033965778 scopus 로고    scopus 로고
    • Expression of a new operon from Bacillus subtilis, ykzB-ykoL, under the control of the TnrA and PhoP-PhoR global regulators
    • Robichon, D., M. Arnaud, R. Gardan, Z. Pragai, M. O'Reilly, G. Rapoport, and M. Debarbouille. 2000. Expression of a new operon from Bacillus subtilis, ykzB-ykoL, under the control of the TnrA and PhoP-PhoR global regulators. J. Bacteriol. 182:1226-1231.
    • (2000) J. Bacteriol. , vol.182 , pp. 1226-1231
    • Robichon, D.1    Arnaud, M.2    Gardan, R.3    Pragai, Z.4    O'Reilly, M.5    Rapoport, G.6    Debarbouille, M.7
  • 39
    • 0026195971 scopus 로고
    • Dependence of Bacillus subtilis cell respiration on monovalent cations
    • Samuilov, V. D., and S. A. Khakimov. 1991. Dependence of Bacillus subtilis cell respiration on monovalent cations. Biokhimiia 56:1209-1214.
    • (1991) Biokhimiia , vol.56 , pp. 1209-1214
    • Samuilov, V.D.1    Khakimov, S.A.2
  • 41
    • 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
  • 42
    • 0032189445 scopus 로고    scopus 로고
    • Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential
    • Schirawski, J., and G. Unden. 1998. Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential. Eur. J. Biochem. 257:210-215.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 210-215
    • Schirawski, J.1    Unden, G.2
  • 43
    • 0023192483 scopus 로고
    • Cloning and nucleotide sequence of phoP, the regulatory gene for alkaline phosphatase and phosphodiesterase in Bacillus subtilis
    • Seki, T., H. Yoshikawa, H. Takahashi, and H. Saito. 1987. Cloning and nucleotide sequence of phoP, the regulatory gene for alkaline phosphatase and phosphodiesterase in Bacillus subtilis. J. Bacteriol. 169:2913-2916.
    • (1987) J. Bacteriol. , vol.169 , pp. 2913-2916
    • Seki, T.1    Yoshikawa, H.2    Takahashi, H.3    Saito, H.4
  • 44
    • 0032920056 scopus 로고    scopus 로고
    • The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of Pho regulon genes in Bacillus subtilis
    • Shi, L., and F. M. Hulett. 1999. The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of Pho regulon genes in Bacillus subtilis. Mol. Microbiol. 31:211-222.
    • (1999) Mol. Microbiol. , vol.31 , pp. 211-222
    • Shi, L.1    Hulett, F.M.2
  • 45
    • 0022445885 scopus 로고
    • Construction of a single-copy integration vector and its use in analysis of regulation of the trp operon of Bacillus subtilis
    • Shimotsu, H., and D. J. Henner. 1986. Construction of a single-copy integration vector and its use in analysis of regulation of the trp operon of Bacillus subtilis. Gene 43:85-94.
    • (1986) Gene , vol.43 , pp. 85-94
    • Shimotsu, H.1    Henner, D.J.2
  • 47
    • 0028354905 scopus 로고
    • Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination
    • Steinmetz, M., and R. Richter. 1994. Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination. Gene 142:79-83.
    • (1994) Gene , vol.142 , pp. 79-83
    • Steinmetz, M.1    Richter, R.2
  • 48
    • 0027506115 scopus 로고
    • Transition-state regulators: Sentinels of Bacillus subtilis post-exponential gene expression
    • Strauch, M. A., and J. A. Hoch. 1993. Transition-state regulators: sentinels of Bacillus subtilis post-exponential gene expression. Mol. Microbiol. 7:337-342.
    • (1993) Mol. Microbiol. , vol.7 , pp. 337-342
    • Strauch, M.A.1    Hoch, J.A.2
  • 49
    • 0029966440 scopus 로고    scopus 로고
    • Three two-component signal-transduction systems interact for Pho regulation in Bacillus subtilis
    • Sun, G., S. M. Birkey, and F. M. Hulett. 1996. Three two-component signal-transduction systems interact for Pho regulation in Bacillus subtilis. Mol. Microbiol. 19:941-948.
    • (1996) Mol. Microbiol. , vol.19 , pp. 941-948
    • Sun, G.1    Birkey, S.M.2    Hulett, F.M.3
  • 51
    • 0028046467 scopus 로고
    • Bacillus subtilis CtaA is a heme-containing membrane protein involved in heme A biosynthesis
    • Svensson, B., and L. Hederstedt. 1994. Bacillus subtilis CtaA is a heme-containing membrane protein involved in heme A biosynthesis. J. Bacteriol. 176:6663-6671.
    • (1994) J. Bacteriol. , vol.176 , pp. 6663-6671
    • Svensson, B.1    Hederstedt, L.2
  • 52
    • 0027527547 scopus 로고
    • Bacillus subtilis CtaA and CtaB function in haem A biosynthesis
    • Svensson, B., M. Lubben, and L. Hederstedt. 1993. Bacillus subtilis CtaA and CtaB function in haem A biosynthesis. Mol. Microbiol. 10:193-201.
    • (1993) Mol. Microbiol. , vol.10 , pp. 193-201
    • Svensson, B.1    Lubben, M.2    Hederstedt, L.3
  • 53
  • 54
    • 0032415869 scopus 로고    scopus 로고
    • Cytochrome bd biosynthesis in Bacillus subtilis: Characterization of the cydABCD operon
    • Winstedt, L., K. Yoshida, Y. Fujita, and C. von Wachenfeldt. 1998. Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon. J. Bacteriol. 180:6571-6580.
    • (1998) J. Bacteriol. , vol.180 , pp. 6571-6580
    • Winstedt, L.1    Yoshida, K.2    Fujita, Y.3    Von Wachenfeldt, C.4
  • 55
    • 0028840368 scopus 로고
    • The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization
    • Yu, J., L. Hederstedt, and P. Piggot. 1995. The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization. J. Bacteriol. 177:6751-6760.
    • (1995) J. Bacteriol. , vol.177 , pp. 6751-6760
    • Yu, J.1    Hederstedt, L.2    Piggot, P.3
  • 56
    • 0033822093 scopus 로고    scopus 로고
    • ResD signal transduction regulator of aerobic respiration in Bacillus subtilis: ctaA promoter regulation
    • Zhang, X., and F. M. Hulett. 2000. ResD signal transduction regulator of aerobic respiration in Bacillus subtilis: ctaA promoter regulation. Mol. Microbiol. 37:1208-1219.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1208-1219
    • Zhang, X.1    Hulett, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.