메뉴 건너뛰기




Volumn 2, Issue 12, 2004, Pages 954-966

Bacterial redox sensors

Author keywords

[No Author keywords available]

Indexed keywords

1,4 BENZOQUINONE; 5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ACONITATE HYDRATASE; CYSTEINE; DNA; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; HEME; IRON SULFUR PROTEIN; MENADIONE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NITRIC OXIDE REDUCTASE; OXIDOREDUCTASE; PEROXIDE; PYRIDINE NUCLEOTIDE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REX PROTEIN; SUPEROXIDE DISMUTASE;

EID: 9444239308     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1022     Document Type: Review
Times cited : (336)

References (120)
  • 1
    • 0032724622 scopus 로고    scopus 로고
    • Mechanisms for redox control of gene expression
    • Bauer, C., Elsen, S. & Bird, T. H. Mechanisms for redox control of gene expression. Annu. Rev. Microbiol. 53, 495-523 (1999).
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 495-523
    • Bauer, C.1    Elsen, S.2    Bird, T.H.3
  • 2
    • 0004268763 scopus 로고    scopus 로고
    • (eds Storz, G. & Hengge-Aronis, R.) (ASM, Washington DC)
    • Storz, G. & Zheng, M. in Bacterial Stress Responses (eds Storz, G. & Hengge-Aronis, R.) 47-59 (ASM, Washington DC, 2000).
    • (2000) Bacterial Stress Responses , pp. 47-59
    • Storz, G.1    Zheng, M.2
  • 4
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley, P. J. & Beinert, H. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6, 181-185 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 6
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M. et al. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183, 4562-4570 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1
  • 7
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G., Tartaglia, L. A. & Ames, B. N. Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248, 189-194 (1990).
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 8
    • 0028965108 scopus 로고
    • Mutational analysis of the redox-sensitive transcriptional regulator OxyR: Regions important for oxidation and transcriptional activation
    • Kullik, I., Toledano, M. B., Tartaglia, L. A. & Storz G. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J. Bacteriol. 177, 1275-1284 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 9
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • Hausladen, A., Privalle, C. T., Keng, T., DeAngelo, J. & Stamler, J. S. Nitrosative stress: activation of the transcription factor OxyR. Cell 86, 719-729 (1996).
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    DeAngelo, J.4    Stamler, J.S.5
  • 10
    • 1642514907 scopus 로고    scopus 로고
    • Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species
    • Mukhopadhyay, P., Zheng, M., Bedzyk, L. A., LaRossa, R. A. & Storz, G. Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. Proc. Natl Acad. Sci. USA 101, 745-750 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 745-750
    • Mukhopadhyay, P.1    Zheng, M.2    Bedzyk, L.A.3    LaRossa, R.A.4    Storz, G.5
  • 11
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, F. & Storz, G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721 (1998).
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Åslund, F.2    Storz, G.3
  • 12
    • 0032792514 scopus 로고    scopus 로고
    • In vivo oxidation-reduction kinetics of OxyR, the transcriptional activator for an oxidative stress-inducible regulon in Escherichia coli
    • Tao, K. In vivo oxidation-reduction kinetics of OxyR, the transcriptional activator for an oxidative stress-inducible regulon in Escherichia coli. FESS Lett. 457, 90-92 (1999).
    • (1999) FESS Lett. , vol.457 , pp. 90-92
    • Tao, K.1
  • 13
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Åslund, F., Zheng, M., Beckwith, J. & Storz, G. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc. Natl Acad. Sci. USA 96, 6161-6165 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6161-6165
    • Åslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 14
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi, H. et al. Structural basis of the redox switch in the OxyR transcription factor. Cell 105, 103-113 (2001).
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1
  • 15
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: A molecular code for redox-related signaling
    • Kim, S. O. et al. OxyR: a molecular code for redox-related signaling. Cell 109, 383-396 (2002).
    • (2002) Cell , vol.109 , pp. 383-396
    • Kim, S.O.1
  • 18
    • 0033517138 scopus 로고    scopus 로고
    • RsrA, an anti-sigma factor regulated by redox change
    • Kang, J.-G. et al. RsrA, an anti-sigma factor regulated by redox change. EMBO J. 18, 4292-4298 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4292-4298
    • Kang, J.-G.1
  • 19
    • 0036065206 scopus 로고    scopus 로고
    • H in Mycobacterium tuberculosis global gene expression
    • H in Mycobacterium tuberculosis global gene expression. Mol. Microbiol. 45, 365-374 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 365-374
    • Manganelli, R.1
  • 21
    • 0035116721 scopus 로고    scopus 로고
    • Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch
    • Paget, M. S. B. et al. Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch. Mol. Microbiol. 39, 1036-1047 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 1036-1047
    • Paget, M.S.B.1
  • 22
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulfide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • Li, W. et al. The role of zinc in the disulfide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J. Mol. Biol. 333, 461-472 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 461-472
    • Li, W.1
  • 23
    • 0023968065 scopus 로고
    • Molecular genetics of photosynthetic membrane biosynthesis in Rhodobacter sphaeroides
    • Kiley, P. J. & Kaplan, S. Molecular genetics of photosynthetic membrane biosynthesis in Rhodobacter sphaeroides. Microbiol. Rev. 52, 50-69 (1988).
    • (1988) Microbiol. Rev. , vol.52 , pp. 50-69
    • Kiley, P.J.1    Kaplan, S.2
  • 24
  • 25
    • 0037076333 scopus 로고    scopus 로고
    • Repression of photosynthesis gene expression by formation of a disulfide bond in CrtJ
    • Masuda, S. et al. Repression of photosynthesis gene expression by formation of a disulfide bond in CrtJ. Proc. Natl Acad. Sci. USA 99, 7078-7083 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7078-7083
    • Masuda, S.1
  • 26
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox
    • Zhulin, I. B., Taylor, B. L. & Dixon R. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22, 331-333 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 27
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • Masuda, S. & Bauer, C. E. AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 110, 613-623 (2002).
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 28
    • 0026585783 scopus 로고
    • Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expresson in Rhodobacter capsulatus
    • Sganga, M. W. & Bauer, C. E. Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expresson in Rhodobacter capsulatus. Cell 68, 945-954 (1992).
    • (1992) Cell , vol.68 , pp. 945-954
    • Sganga, M.W.1    Bauer, C.E.2
  • 29
    • 0035946912 scopus 로고    scopus 로고
    • The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus
    • Swem, L. R. et al. The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus. J. Mol. Biol. 309, 121-138 (2001).
    • (2001) J. Mol. Biol. , vol.309 , pp. 121-138
    • Swem, L.R.1
  • 30
    • 0036786855 scopus 로고    scopus 로고
    • Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N
    • Romagnoli, S., Packer, H. L. & Armitage, J. P. Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N. J. Bacteriol. 184, 5590-5598 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 5590-5598
    • Romagnoli, S.1    Packer, H.L.2    Armitage, J.P.3
  • 31
    • 0141848318 scopus 로고    scopus 로고
    • Signal transduction by the global regulator RegB is mediated by a redox-active cysteine
    • Swem, L. R. et al. Signal transduction by the global regulator RegB is mediated by a redox-active cysteine. EMBO J. 22, 4699-4708 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4699-4708
    • Swem, L.R.1
  • 32
    • 0034664042 scopus 로고    scopus 로고
    • Redox signaling: Globalization of gene expression
    • Oh, J. I. & Kaplan, S. Redox signaling: globalization of gene expression. EMBO J. 19, 4237-4247 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4237-4247
    • Oh, J.I.1    Kaplan, S.2
  • 33
    • 2942735337 scopus 로고    scopus 로고
    • Reconstitution of the Rhodobacter sphaeroides cbb3-PrrBA signal transduction pathway in vitro
    • Oh, J. I., Ko, I. J. & Kaplan S. Reconstitution of the Rhodobacter sphaeroides cbb3-PrrBA signal transduction pathway in vitro. Biochemistry 43, 7915-7923 (2004).
    • (2004) Biochemistry , vol.43 , pp. 7915-7923
    • Oh, J.I.1    Ko, I.J.2    Kaplan, S.3
  • 34
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M. & Helmann, J. D. The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl Acad. Sci. USA 99, 6690-6695 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 35
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P. J., Bennik, M. H. J. & Demple, B. Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J. Bacteriol. 183, 3890-3902 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.J.2    Demple, B.3
  • 36
    • 0036365511 scopus 로고    scopus 로고
    • Escherichia coli SoxR protein: Sensor/transducer of oxidative stress and nitric oxide
    • Demple, B., Ding, H. & Jorgensen, M. Escherichia coli SoxR protein: sensor/transducer of oxidative stress and nitric oxide. Methods Enzymol. 348, 355-364 (2002).
    • (2002) Methods Enzymol. , vol.348 , pp. 355-364
    • Demple, B.1    Ding, H.2    Jorgensen, M.3
  • 37
    • 0029152251 scopus 로고
    • Binuclear [2Fe-2S) clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • Hidalgo, E., Bollinger, J. M., Bradley, J. M., Walsh, C. T. & Demple, B. Binuclear [2Fe-2S) clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270, 20908-20914 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger, J.M.2    Bradley, J.M.3    Walsh, C.T.4    Demple, B.5
  • 38
    • 0028929893 scopus 로고
    • Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative stress response regulon in Escherichia coli
    • Wu, J., Dunham, W. R. & Weiss, B. Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative stress response regulon in Escherichia coli. J. Bid. Chem. 270 10323-10327 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 10323-10327
    • Wu, J.1    Dunham, W.R.2    Weiss, B.3
  • 39
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding, H. & Demple, B. In vivo kinetics of a redox-regulated transcriptional switch. Proc. Natl Acad. Sci. USA 94, 8445-8449 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 40
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor SoxR in Escherichia coli
    • Koo, M. S. et al. A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J. 22, 2614-2622 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2614-2622
    • Koo, M.S.1
  • 41
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • Ding, H., Hidalgo, E. & Demple, B. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J. Biol. Chem. 271, 33173-33176 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 33173-33176
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 42
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur clusters in the SoxR transcription activator
    • Ding, H. & Demple, B. Direct nitric oxide signal transduction via nitrosylation of iron-sulfur clusters in the SoxR transcription activator. Proc. Natl Acad. Sci. USA 97, 5146-5150 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 44
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation
    • Unden, G. & Bongaerts, J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation. Biochim. Biophys. Acta 1320, 217-234 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 45
    • 0037357728 scopus 로고    scopus 로고
    • Gene array-based identification of changes that contribute to ethanol tolerance in ethanologenic Escherichia coli: Comparison of KO11 (parent) to LY01 (resistant mutant)
    • Gonzalez, R. et al. Gene array-based identification of changes that contribute to ethanol tolerance in ethanologenic Escherichia coli: comparison of KO11 (parent) to LY01 (resistant mutant). Biotechnol. Prog. 19, 612-623 (2003).
    • (2003) Biotechnol. Prog. , vol.19 , pp. 612-623
    • Gonzalez, R.1
  • 46
    • 0043032584 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coil K12: The effects of oxygen availability and FNR
    • Salmon, K. et al. Global gene expression profiling in Escherichia coil K12: the effects of oxygen availability and FNR. J. Biol. Chem. 278, 29837-29855 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29837-29855
    • Salmon, K.1
  • 47
    • 2342648924 scopus 로고    scopus 로고
    • Integrating high-throughput and computational data elucidates bacterial networks
    • Corvet, M. W., Knight, E. M., Reed, J. L., Herrgard, M. J. & Palsson, B. O. Integrating high-throughput and computational data elucidates bacterial networks. Nature 429, 92-96 (2004).
    • (2004) Nature , vol.429 , pp. 92-96
    • Corvet, M.W.1    Knight, E.M.2    Reed, J.L.3    Herrgard, M.J.4    Palsson, B.O.5
  • 48
    • 0029664739 scopus 로고    scopus 로고
    • 2 as the regulatory signal for FNR-dependent gene expression in Escherichia coli
    • 2 as the regulatory signal for FNR-dependent gene expression in Escherichia coli. J. Bacteriol. 178, 4515-4521 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 4515-4521
    • Becker, S.1    Holighaus, G.2    Gabrielczyk, T.3    Unden, G.4
  • 49
    • 1542364538 scopus 로고    scopus 로고
    • Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR)
    • Crack, J., Green, J. & Thomson, A. J. Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR). J. Biol. Chem. 279, 9278-9286 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 9278-9286
    • Crack, J.1    Green, J.2    Thomson, A.J.3
  • 50
    • 0030695304 scopus 로고    scopus 로고
    • FNR is a direct oxygen sensor having a biphasic response curve
    • Jordan, P. A., Thomson, A. J., Ralph, E. T., Guest, J. R. & Green, J. FNR is a direct oxygen sensor having a biphasic response curve. FEBS Lett. 416, 349-352 (1997).
    • (1997) FEBS Lett. , vol.416 , pp. 349-352
    • Jordan, P.A.1    Thomson, A.J.2    Ralph, E.T.3    Guest, J.R.4    Green, J.5
  • 52
    • 0027451092 scopus 로고
    • The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state
    • Lazazzera, B. A., Bates, D. & Kiley, P. J. The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state. Genes Dev. 7, 1993-2005 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 1993-2005
    • Lazazzera, B.A.1    Bates, D.2    Kiley, P.J.3
  • 53
    • 0030029817 scopus 로고    scopus 로고
    • DNA-binding and dimerization of the Fe-S containing FNR protein Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., Beinert, H., Khoroshilova, N., Kennedy, M. C. & Kiley, P. J. DNA-binding and dimerization of the Fe-S containing FNR protein Escherichia coli are regulated by oxygen. J. Biol. Chem. 271, 2762-2768 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 54
    • 0032505869 scopus 로고    scopus 로고
    • Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli
    • Popescu, C. V., Bates, D. M., Beinert, H., Munck, E. & Kiley, P. J. Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli. Proc. Natl Acad. Sci. USA 95, 13431-13435 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13431-13435
    • Popescu, C.V.1    Bates, D.M.2    Beinert, H.3    Munck, E.4    Kiley, P.J.5
  • 55
    • 0037127302 scopus 로고    scopus 로고
    • Miscoordination of the iron-sulfur clusters of the anaerobic transcription factor FNR allows simple repression but not activation
    • Scott, C. & Green, J. Miscoordination of the iron-sulfur clusters of the anaerobic transcription factor FNR allows simple repression but not activation. J. Biol. Chem. 277, 1749-1754 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1749-1754
    • Scott, C.1    Green, J.2
  • 56
    • 0035824571 scopus 로고    scopus 로고
    • Characterization of the dimerization domain in the FNR transcription factor
    • Moore, L. J. & Kiley, P. J. Characterization of the dimerization domain in the FNR transcription factor. J. Biol. Chem. 276, 45744-45750 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 45744-45750
    • Moore, L.J.1    Kiley, P.J.2
  • 57
    • 0025853723 scopus 로고
    • Characterization of the FNR protein of Escherichia coli, an iron binding transcriptional regulator
    • Green, J., Trageser, M., Six, S., Unden, G. & Guest, J. R. Characterization of the FNR protein of Escherichia coli, an iron binding transcriptional regulator. Proc. R. Soc. Lond. B. 244 137-144 (1991).
    • (1991) Proc. R. Soc. Lond. B. , vol.244 , pp. 137-144
    • Green, J.1    Trageser, M.2    Six, S.3    Unden, G.4    Guest, J.R.5
  • 58
    • 1642453843 scopus 로고    scopus 로고
    • 2+ cluster of FNR from Escherichia coli
    • 2+ cluster of FNR from Escherichia coli. Biochemistry 43, 791-798 (2004).
    • (2004) Biochemistry , vol.43 , pp. 791-798
    • Sutton, V.R.1
  • 59
    • 0034008659 scopus 로고    scopus 로고
    • 2+ cluster to oxygen
    • 2+ cluster to oxygen. J. Biol. Chem. 276, 6234-6240 (2000).
    • (2000) J. Biol. Chem. , vol.276 , pp. 6234-6240
    • Bates, D.M.1
  • 60
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C. J. et al. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl Acad. Sci. USA 98, 14895-14900 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1
  • 61
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S1 cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro
    • Green, J. et al. Reconstitution of the [4Fe-4S1 cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro. Biochem. J. 316, 887-892 (1996).
    • (1996) Biochem. J. , vol.316 , pp. 887-892
    • Green, J.1
  • 62
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA-binding
    • Khoroshilova, N., Beinert, H. & Kiley, F. J. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA-binding. Proc. Natl Acad. Sci. USA 92, 2499-2505 (1995 ).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2499-2505
    • Khoroshilova, N.1    Beinert, H.2    Kiley, F.J.3
  • 63
    • 0036646484 scopus 로고    scopus 로고
    • NO sensing by FNR: Regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp
    • Cruz-Ramos, H. et al. NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J. 21, 3235-3244 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3235-3244
    • Cruz-Ramos, H.1
  • 64
    • 0034072208 scopus 로고    scopus 로고
    • New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress
    • Poole, R. K. & Hughes, M. N. New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress. Mol. Microbiol. 36, 775-783 (2000).
    • (2000) Mol. Microbiol. , vol.36 , pp. 775-783
    • Poole, R.K.1    Hughes, M.N.2
  • 65
    • 0033621064 scopus 로고    scopus 로고
    • Bacillus subtilis aconitase is an RNA-binding protein
    • Alen, C. & Sonenshein, A. L. Bacillus subtilis aconitase is an RNA-binding protein. Proc. Natl Acad. Sci. USA 96, 10412-10417 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10412-10417
    • Alen, C.1    Sonenshein, A.L.2
  • 66
    • 0032739921 scopus 로고    scopus 로고
    • Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
    • Tang, Y. & Guest, J. R. Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145, 3069-3079 (1999).
    • (1999) Microbiology , vol.145 , pp. 3069-3079
    • Tang, Y.1    Guest, J.R.2
  • 67
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: Post-transcriptional regulation of sodA expression
    • Tang, Y., Quail, M. A., Artymiuk, P. J., Guest, J. R. & Green, J. Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148, 1027-1037 (2002).
    • (2002) Microbiology , vol.148 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Guest, J.R.4    Green, J.5
  • 68
    • 1642565352 scopus 로고    scopus 로고
    • Post-transcriptional regulation of bacterial motility by aconitase proteins
    • Tang, Y., Guest, J. R., Artymiuk, P. J., Read, R. C. & Green, J. Post-transcriptional regulation of bacterial motility by aconitase proteins. Mol. Microbiol. 51, 1817-1826 (2004).
    • (2004) Mol. Microbiol. , vol.51 , pp. 1817-1826
    • Tang, Y.1    Guest, J.R.2    Artymiuk, P.J.3    Read, R.C.4    Green, J.5
  • 69
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme and iron-regulatory protein
    • Beinert, H., Kennedy, M. C. & Stout, C. D. Aconitase as iron-sulfur protein, enzyme and iron-regulatory protein. Chem. Rev. 96, 2335-2373 (1996).
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2373
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 70
    • 0036260715 scopus 로고    scopus 로고
    • E. coli aconitase B structure reveals a HEAT-like domain with implication for protein-protein recognition
    • Williams, C. H. et al. E. coli aconitase B structure reveals a HEAT-like domain with implication for protein-protein recognition. Nature Struct. Biol. 9, 447-452 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 447-452
    • Williams, C.H.1
  • 71
    • 0031438608 scopus 로고    scopus 로고
    • Transcriptional regulation of the aconitase genes (acn4 and acnB) of Escherichia coli
    • Cunningham, L., Gruer, M. J. & Guest, J. R. Transcriptional regulation of the aconitase genes (acn4 and acnB) of Escherichia coli. Microbiology 143, 3795-3805 (1997).
    • (1997) Microbiology , vol.143 , pp. 3795-3805
    • Cunningham, L.1    Gruer, M.J.2    Guest, J.R.3
  • 72
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. & Fridovich, I. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266, 19328-19333 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 73
    • 0026806913 scopus 로고
    • Inactivation-reactivation of aconitase in Escherichia coli: A sensitive measure of superoxide radical
    • Gardner, P. R. & Fridovich, I. Inactivation-reactivation of aconitase in Escherichia coli: a sensitive measure of superoxide radical. J. Biol. Chem. 267, 8757-8763 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 8757-8763
    • Gardner, P.R.1    Fridovich, I.2
  • 74
  • 76
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese, S., Tang, Y. & Imlay, J. A. Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185, 221-230 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 77
    • 0035910067 scopus 로고    scopus 로고
    • Feedback regulation of iron-sulfur cluster biosynthesis
    • Frazzon, J. & Dean, D. R. Feedback regulation of iron-sulfur cluster biosynthesis. Proc. Natl Acad. Sci. USA 98, 14751-14753 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14751-14753
    • Frazzon, J.1    Dean, D.R.2
  • 78
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz, C. J., Djaman, O., Imlay, J. A. & Kiley, P. J. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl Acad. Sci. USA 97, 9009-9014 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 79
    • 0028108941 scopus 로고
    • Genetic-regulation of nitrogen fixation in Rhizobia
    • Fischer, H. M. Genetic-regulation of nitrogen fixation in Rhizobia. Microbiol. Rev. 58, 352-386 (1994).
    • (1994) Microbiol. Rev. , vol.58 , pp. 352-386
    • Fischer, H.M.1
  • 80
    • 0032438105 scopus 로고    scopus 로고
    • Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction
    • Gong, W. M. et al. Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc. Natl Acad Sci. USA 95, 15177-15182 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15177-15182
    • Gong, W.M.1
  • 81
    • 0028949951 scopus 로고
    • Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron
    • Gilles-Gonzalez, M. A., Gonzalez, G. & Perutz, M. F. Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 34, 232-236 (1995).
    • (1995) Biochemistry , vol.34 , pp. 232-236
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 82
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon, V. M., Gonzalez, G. & Gilles-Gonzalez, M. A. Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39, 2685-2691 (2000).
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 83
    • 0037008046 scopus 로고    scopus 로고
    • Nature of the displaceable heme axial residue in the EcDos protein, a heme-based sensor from Escherichia coli
    • Gonzalez, G. et al. Nature of the displaceable heme axial residue in the EcDos protein, a heme-based sensor from Escherichia coli. Biochemistry 41, 8414-8421 (2002).
    • (2002) Biochemistry , vol.41 , pp. 8414-8421
    • Gonzalez, G.1
  • 84
    • 0037031927 scopus 로고    scopus 로고
    • Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli
    • Sato, A. et al. Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli. J. Biol. Chem. 277 32650-32658 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 32650-32658
    • Sato, A.1
  • 85
    • 0038052346 scopus 로고    scopus 로고
    • Ligand binding dynamics to the heme domain of the oxygen sensor Dos from Escherichia coli
    • Liebl, U. et al. Ligand binding dynamics to the heme domain of the oxygen sensor Dos from Escherichia coli. Biochemistry 42, 6527-6535 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6527-6535
    • Liebl, U.1
  • 86
    • 0037189552 scopus 로고    scopus 로고
    • Characterization of a direct oxygen sensor heme protein from Escherichia coli
    • Sasakura, Y et al. Characterization of a direct oxygen sensor heme protein from Escherichia coli. J. Biol. Chem. 277 23821-23827 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 23821-23827
    • Sasakura, Y.1
  • 87
    • 0346732270 scopus 로고    scopus 로고
    • Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants
    • Yoshimura, T., Sagami, I., Sasakura Y. & Shimizu T. Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli a study of deletion and site-directed mutants. J. Biol. Chem. 278, 53105-53111 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 53105-53111
    • Yoshimura, T.1    Sagami, I.2    Sasakura, Y.3    Shimizu, T.4
  • 88
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing home proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (EcDosH)
    • Park, H. J., Suquet, C., Satterlee, J. D. & Kang, C. H. Insights into signal transduction involving PAS domain oxygen-sensing home proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (EcDosH). Biochemistry 43, 2738-2746 (2004 ).
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.J.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.H.4
  • 89
    • 2442624510 scopus 로고    scopus 로고
    • A redox-oontrolled molecular switch revealed by the crystal structure of a bacterial herme PAS sensor
    • Kurokawa, H. et al. A redox-oontrolled molecular switch revealed by the crystal structure of a bacterial herme PAS sensor. J. Biol. Chem. 279, 20186-20193 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 20186-20193
    • Kurokawa, H.1
  • 90
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and Bacteria
    • Hou, S. et al. Myoglobin-like aerotaxis transducers in Archaea and Bacteria. Nature 403, 540-544 (2000).
    • (2000) Nature , vol.403 , pp. 540-544
    • Hou, S.1
  • 91
    • 0035979209 scopus 로고    scopus 로고
    • Globin-coupled sensors: A class of heme-containing sensors in Archaea and Bacteria
    • Hou, S. B. et al. Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria. Proc. Natl Acad. Sci. USA 98, 9353-9358 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9353-9358
    • Hou, S.B.1
  • 92
    • 0042334880 scopus 로고    scopus 로고
    • Structure of the oxygen sensor in Bacillus subtilis: Signal transduction of chemotaxis by control of symmetry
    • Zhang, W. & Phillips, G. N. Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry. Structure 11, 1097-1110 (2003).
    • (2003) Structure , vol.11 , pp. 1097-1110
    • Zhang, W.1    Phillips, G.N.2
  • 93
    • 1642500165 scopus 로고    scopus 로고
    • The NifL-NifA system: A multidomain transcriptional regulatory complex that integrates environmental signals
    • Martinez-Argudo, I., Little, R., Shearer, N., Johnson, P. & Dixon, R. The NifL-NifA system: a multidomain transcriptional regulatory complex that integrates environmental signals. J. Bacteriol. 186 601-610 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 601-610
    • Martinez-Argudo, I.1    Little, R.2    Shearer, N.3    Johnson, P.4    Dixon, R.5
  • 94
    • 0029875231 scopus 로고    scopus 로고
    • Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
    • Hill, S., Austin, S., Eydmann, T., Jones, T. & Dixon, R. Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch. Proc. Natl Acad. Sci. USA 93, 2143-2148 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 95
    • 9344269892 scopus 로고    scopus 로고
    • Iron is required to relieve inhibitory effects on NifL on transcriptional activation by NifA in Klebsiella pneumoniae
    • Schmitz, R., He, L. & Kustu, S. Iron is required to relieve inhibitory effects on NifL on transcriptional activation by NifA in Klebsiella pneumoniae. J. Bacteriol. 178, 4679-4687 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 4679-4687
    • Schmitz, R.1    He, L.2    Kustu, S.3
  • 96
    • 0032103448 scopus 로고    scopus 로고
    • Electron donation to the flavoprotein NifL, a redox sensing transcription regulator
    • Macheroux, P. et al. Electron donation to the flavoprotein NifL, a redox sensing transcription regulator. Biochem. J. 332, 413-419 (1998).
    • (1998) Biochem. J. , vol.332 , pp. 413-419
    • Macheroux, P.1
  • 97
    • 0035140627 scopus 로고    scopus 로고
    • Fnr is required for NifL-dependent oxygen control of nif gene expression in Klebsiella prieumoniae
    • Grabbe, R., Klopprogge, K. & Schmitz, R. A. Fnr is required for NifL-dependent oxygen control of nif gene expression in Klebsiella prieumoniae. J. Bacteriol. 183, 1385-1393 (2001 ).
    • (2001) J. Bacteriol. , vol.183 , pp. 1385-1393
    • Grabbe, R.1    Klopprogge, K.2    Schmitz, R.A.3
  • 98
    • 0037392283 scopus 로고    scopus 로고
    • Oxygen control of nif gene expression in Klebsiella pneumoniae depends on NifL reduction at the cytoplasmic membrane by electrons derived from the reduced quinone pool
    • Grabbe, R. & Schmitz R. A. Oxygen control of nif gene expression in Klebsiella pneumoniae depends on NifL reduction at the cytoplasmic membrane by electrons derived from the reduced quinone pool. Eur. J. Biochem. 270, 1555-1566 (2003).
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1555-1566
    • Grabbe, R.1    Schmitz, R.A.2
  • 99
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the Serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behaviour
    • Rebbapragada, A. et al. The Aer protein and the Serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behaviour. Proc. Natl Acad. Sci. USA 94, 10541-10546 (1997 ).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1
  • 100
    • 0034705035 scopus 로고    scopus 로고
    • Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli
    • Bibikov, S. I., Barnes, L. A., Gitin, Y. & Parkinson, J. S. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli. Proc. Natl Acad. Sci. USA 97, 5830-5835 (2000)
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5830-5835
    • Bibikov, S.I.1    Barnes, L.A.2    Gitin, Y.3    Parkinson, J.S.4
  • 101
    • 0034029031 scopus 로고    scopus 로고
    • PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli
    • Repik, A. et al. PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli. Mol. Microbiol. 36, 806-816 (2000).
    • (2000) Mol. Microbiol. , vol.36 , pp. 806-816
    • Repik, A.1
  • 102
    • 0015365891 scopus 로고
    • Levels of nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide in facultative bacteria and the effect of oxygen
    • Wimpenny, J. W. & Firth, A. Levels of nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide in facultative bacteria and the effect of oxygen. J. Bacteriol. 111, 24-32 (1972).
    • (1972) J. Bacteriol. , vol.111 , pp. 24-32
    • Wimpenny, J.W.1    Firth, A.2
  • 104
    • 0037072770 scopus 로고    scopus 로고
    • Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron
    • Woodmansee, A. N. & Imlay, J. A. Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron. J. Biol. Chem. 277, 34055-34066 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34055-34066
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 107
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A. M. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5, 775-783 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 109
    • 0030984442 scopus 로고    scopus 로고
    • In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli
    • Georgellis, D., Lynch, A. S. & Lin, E. C. C. In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli. J. Bacteriol. 179, 5429-5435 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5429-5435
    • Georgellis, D.1    Lynch, A.S.2    Lin, E.C.C.3
  • 110
    • 0034123699 scopus 로고    scopus 로고
    • Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli
    • Kwon, O., Georgellis, D. & Lin, E. C. C. Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli. J. Bacteriol. 182, 3858-3862 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 3858-3862
    • Kwon, O.1    Georgellis, D.2    Lin, E.C.C.3
  • 111
    • 1842529555 scopus 로고    scopus 로고
    • Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling
    • Liu, X. & De Wulf, P. Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling. J. Biol. Chem. 279, 12588-12597 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12588-12597
    • Liu, X.1    De Wulf, P.2
  • 112
    • 0024121496 scopus 로고
    • arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways
    • Iuchi, S. & Lin, E. C. C. arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways. Proc. Natl Acad. Sci. USA 85, 1888-1892 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1888-1892
    • Iuchi, S.1    Lin, E.C.C.2
  • 113
    • 0035933597 scopus 로고    scopus 로고
    • Quinones as the redox signal for the arc two-component system of bacteria
    • Georgellis, D., Kwon, O. & Lin, E. C. C. Quinones as the redox signal for the arc two-component system of bacteria. Science 292, 2314-2316 (2001).
    • (2001) Science , vol.292 , pp. 2314-2316
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3
  • 114
    • 4444236656 scopus 로고    scopus 로고
    • Identification of a quinone-sensitive redox switch in the ArcB sensor kinase
    • Malpica, R., Franco, B., Rodriguez, C. & Georgellis, D. Identification of a quinone-sensitive redox switch in the ArcB sensor kinase. Proc. Natl Acad Sci. USA 101, 13318-13323 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13318-13323
    • Malpica, R.1    Franco, B.2    Rodriguez, C.3    Georgellis, D.4
  • 115
    • 0033544879 scopus 로고    scopus 로고
    • Amplification of signalling activity of the arc two-component system of Escherichia coli by anaerobic metabolites. An in vitro study with different protein modules
    • Georgellis, D., Kwon, O. & Lin, E. C. C. Amplification of signalling activity of the arc two-component system of Escherichia coli by anaerobic metabolites. An in vitro study with different protein modules. J. Biol. Chem. 274, 35950-35954 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35950-35954
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3
  • 116
    • 1642282533 scopus 로고    scopus 로고
    • Effect of D-lactate on the physiological activity of the ArcB sensor kinase in Escherichia coli
    • Rodriguez, C., Kwon, O. & Georgellis, D. Effect of D-lactate on the physiological activity of the ArcB sensor kinase in Escherichia coli. J. Bacteriol. 186, 2085-2090 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 2085-2090
    • Rodriguez, C.1    Kwon, O.2    Georgellis, D.3
  • 117
    • 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. & Gross, R. The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier. Eur. J. Biochem. 259, 3479-3484 (2002).
    • (2002) Eur. J. Biochem. , vol.259 , pp. 3479-3484
    • Bock, A.1    Gross, R.2
  • 118
    • 0030045823 scopus 로고    scopus 로고
    • Phosphorylated BvgA is sufficient for transcriptional activation of virulence-regulated genes in Bordetella pertussis
    • Steffen, P., Goyard, S. & Ullmann, A. Phosphorylated BvgA is sufficient for transcriptional activation of virulence-regulated genes in Bordetella pertussis. EMBO J. 15, 102-109 (1996).
    • (1996) EMBO J. , vol.15 , pp. 102-109
    • Steffen, P.1    Goyard, S.2    Ullmann, A.3
  • 119
    • 0033538048 scopus 로고    scopus 로고
    • The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
    • Messner, K. R. & Imlay, J. A. The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J. Biol. Chem. 274, 10119-10128 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10119-10128
    • Messner, K.R.1    Imlay, J.A.2
  • 120
    • 0035985581 scopus 로고    scopus 로고
    • How oxygen damages microbes: Oxygen tolerance and obligate anaerobiosis
    • Imlay, J. A. How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Adv. Microbial Phys. 46, 111-153 (2002).
    • (2002) Adv. Microbial Phys. , vol.46 , pp. 111-153
    • Imlay, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.