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Volumn 144, Issue 3, 1998, Pages 705-717

A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei

Author keywords

CRP; FNR; Lactic acid bacteria; Redox sensing; Transcription regulation

Indexed keywords

BACTERIAL PROTEIN; COPPER; CYCLIC AMP; DNA BINDING PROTEIN; FUMARIC ACID; NITRATE; RECEPTOR PROTEIN; TRANSCRIPTION FACTOR; ZINC;

EID: 0031882182     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-144-3-705     Document Type: Article
Times cited : (58)

References (47)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory properties and protective roles in starved Escherichia coli
    • Almirón, M., Link, A. J., Furlong, D. & Kolter, R. (1992). A novel DNA-binding protein with regulatory properties and protective roles in starved Escherichia coli. Genes Dev 6, 2646-2654.
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 2
    • 0029090977 scopus 로고
    • Selection of protein binding sites from random nucleic acid sequences
    • Blackwell, T. K. (1995). Selection of protein binding sites from random nucleic acid sequences. Methods Enzymol 254, 604-618.
    • (1995) Methods Enzymol , vol.254 , pp. 604-618
    • Blackwell, T.K.1
  • 3
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline-phosphatase conjugated anti-antibody on Western blots
    • Blake, M. S., Johnson, K. H., Rassec-Jones, G. W. & Golschlick, E. C. (1984). A rapid, sensitive method for detection of alkaline-phosphatase conjugated anti-antibody on Western blots. Anal Biochem 136, 175-179.
    • (1984) Anal Biochem , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnson, K.H.2    Rassec-Jones, G.W.3    Golschlick, E.C.4
  • 4
    • 0030786451 scopus 로고    scopus 로고
    • DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli
    • Bougerie, S. J., Michán, C. M., Thomas, M. S., Busby, S. J. W. & Hyde, E. I. (1997). DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli. Nucleic Acid Res 25, 1685-1693.
    • (1997) Nucleic Acid Res , vol.25 , pp. 1685-1693
    • Bougerie, S.J.1    Michán, C.M.2    Thomas, M.S.3    Busby, S.J.W.4    Hyde, E.I.5
  • 5
    • 0025830469 scopus 로고
    • A method of identifying protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U., Lüthy, R. & Eisenberg, D. (1991). A method of identifying protein sequences that fold into a known three-dimensional structure. Science 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Lüthy, R.2    Eisenberg, D.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0001978472 scopus 로고    scopus 로고
    • The CAP modulon
    • Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company
    • Busby, S. & Kolb, A. (1996). The CAP modulon. In Regulation of Gene Expression in Escherichia coli, pp. 255-279. Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 255-279
    • Busby, S.1    Kolb, A.2
  • 8
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps(PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • Chen, L. & Helmann, J. D. (1995). Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Mol Microbiol 18, 295-300.
    • (1995) Mol Microbiol , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 9
    • 0001209457 scopus 로고
    • Responses of lactic acid bacteria to oxygen
    • Condon, S. (1987). Responses of lactic acid bacteria to oxygen. FEMS Microbiol Rev 46, 269-280.
    • (1987) FEMS Microbiol Rev , vol.46 , pp. 269-280
    • Condon, S.1
  • 10
    • 0027181941 scopus 로고
    • Progress and potential in the biotechnology of lactic acid bacteria
    • Gasson, M. J. (1993). Progress and potential in the biotechnology of lactic acid bacteria. FEMS Microbiol Rev 12, 3-20.
    • (1993) FEMS Microbiol Rev , vol.12 , pp. 3-20
    • Gasson, M.J.1
  • 11
    • 0024371624 scopus 로고
    • Binding of the Escherichia coli cyclic-AMP receptor protein to DNA fragments containing consensus nucleotide-sequences
    • Gaston, K., Kolb, A. & Busby, S. (1989). Binding of the Escherichia coli cyclic-AMP receptor protein to DNA fragments containing consensus nucleotide-sequences. Biochem J 261, 649-653.
    • (1989) Biochem J , vol.261 , pp. 649-653
    • Gaston, K.1    Kolb, A.2    Busby, S.3
  • 12
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by kinase FixL, are a new class of heme protein with distinctive ligand-binding and autoxidation
    • Gilles-Gonzalez, M. A., Gonzalez, G., Perutz, M. F., Kiger, L. & Poyart, C. (1994). Heme-based sensors, exemplified by kinase FixL, are a new class of heme protein with distinctive ligand-binding and autoxidation. Biochemistry 33, 8067-8073.
    • (1994) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3    Kiger, L.4    Poyart, C.5
  • 13
    • 0027474352 scopus 로고
    • Properties of FNR proteins substituted at each of the five cysteine residues
    • Green, J., Sharrocks, A. D., Green, B., Geisow, M. & Guest, J. R. (1993). Properties of FNR proteins substituted at each of the five cysteine residues. Mol Microbiol 8, 61-68.
    • (1993) Mol Microbiol , vol.8 , pp. 61-68
    • Green, J.1    Sharrocks, A.D.2    Green, B.3    Geisow, M.4    Guest, J.R.5
  • 14
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro
    • Green, J., Bennett, B., Jordan, P., Ralph, E. T., Thomson, A. J. & Guest, J. R. (1996). Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro. Biochem J 316, 887-892.
    • (1996) Biochem J , vol.316 , pp. 887-892
    • Green, J.1    Bennett, B.2    Jordan, P.3    Ralph, E.T.4    Thomson, A.J.5    Guest, J.R.6
  • 15
    • 0001947282 scopus 로고    scopus 로고
    • The FNR modulon and FNR-regulated gene expression
    • Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company
    • Guest, J. R., Green, J., Irvine, A. S. & Spiro, S. (1996). The FNR modulon and FNR-regulated gene expression. In Regulation of Gene Expression in Escherichia coli, pp. 317-342. Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 317-342
    • Guest, J.R.1    Green, J.2    Irvine, A.S.3    Spiro, S.4
  • 16
    • 0030912902 scopus 로고    scopus 로고
    • Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
    • Hildago, E., Ding, H. & Demple, B. (1997). Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem Sci 22, 207-210.
    • (1997) Trends Biochem Sci , vol.22 , pp. 207-210
    • Hildago, E.1    Ding, H.2    Demple, B.3
  • 17
    • 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. (1996). 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) 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
  • 18
    • 0027155055 scopus 로고
    • Lactobacillus casei contains a member of the CRP-FNR family
    • Irvine, A. S. & Guest, J. R. (1993). Lactobacillus casei contains a member of the CRP-FNR family. Nucleic Acid Res 21, 753.
    • (1993) Nucleic Acid Res , vol.21 , pp. 753
    • Irvine, A.S.1    Guest, J.R.2
  • 19
    • 0029155379 scopus 로고
    • Electrophoretic mobility shift assay
    • Kerr, L. D. (1995). Electrophoretic mobility shift assay. Methods Enzymol 254, 619-631.
    • (1995) Methods Enzymol , vol.254 , pp. 619-631
    • Kerr, L.D.1
  • 20
    • 0028965108 scopus 로고
    • Mutational analysis of the redox-sensitive transcriptional regulator OxyR: Regions important for oxidation and transcriptional activation
    • Kullik, I., Toledano, M. B., Yartaglia, L. A. & Storz, G. (1995). Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J Bacteriol 177, 1275-1284.
    • (1995) J Bacteriol , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Yartaglia, L.A.3    Storz, G.4
  • 21
    • 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
  • 22
    • 0030029817 scopus 로고    scopus 로고
    • DNA-binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., Beinert, H., Khoroshilova, N., Kennedy, M. C. & Kiley, P. J. (1996). DNA-binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 271, 2762-2768.
    • (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
  • 23
    • 0025707308 scopus 로고
    • Comparison of promoter activities in Escherichia coli and Pseudomonas aeruginosa - Use of a new broad-host-range promoter-probe plasmid
    • Lodge, J., Williams, R., Bell, A., Chan, B. & Busby, S. (1990). Comparison of promoter activities in Escherichia coli and Pseudomonas aeruginosa - use of a new broad-host-range promoter-probe plasmid. FEMS Microbiol Lett 67, 221-225.
    • (1990) FEMS Microbiol Lett , vol.67 , pp. 221-225
    • Lodge, J.1    Williams, R.2    Bell, A.3    Chan, B.4    Busby, S.5
  • 25
    • 0003162406 scopus 로고    scopus 로고
    • Regulation of aerobic and anaerobic metabolism by the Arc system
    • Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company
    • Lynch, S. A. & Lin, E. C. C. (1996b). Regulation of aerobic and anaerobic metabolism by the Arc system. In Regulation of Gene Expression in Escherichia coli, pp. 361-381. Edited by E. C. C. Lin & S. A. Lynch. Austin, TX: R. G. Landes Company.
    • (1996) Regulation of Gene Expression in Escherichia Coli , pp. 361-381
    • Lynch, S.A.1    Lin, E.C.C.2
  • 26
    • 0023056691 scopus 로고
    • ptac-85, an Escherichia coli vector for expression of non-fusion proteins
    • Marsh, P. (1986). ptac-85, an Escherichia coli vector for expression of non-fusion proteins. Nucleic Acids Res 14, 3603.
    • (1986) Nucleic Acids Res , vol.14 , pp. 3603
    • Marsh, P.1
  • 27
  • 28
    • 0028964123 scopus 로고
    • The oxygen sensor protein, FixL, of Rhizobium meliloti. Role of histidine residues in heme-binding, phosphorylation, and signal-transduction
    • Monson, E. K., Ditta, G. S. & Helinski, D. R. (1995). The oxygen sensor protein, FixL, of Rhizobium meliloti. Role of histidine residues in heme-binding, phosphorylation, and signal-transduction. J Biol Chem 270, 5243-5250.
    • (1995) J Biol Chem , vol.270 , pp. 5243-5250
    • Monson, E.K.1    Ditta, G.S.2    Helinski, D.R.3
  • 29
    • 0025141538 scopus 로고
    • Nucleotide sequences and genomic constitution of five tryptophan genes of Lactobacillus casei
    • Natori, Y., Kano, Y. & Imamoto, F. (1990). Nucleotide sequences and genomic constitution of five tryptophan genes of Lactobacillus casei. J Bacteriol 107, 248-255.
    • (1990) J Bacteriol , vol.107 , pp. 248-255
    • Natori, Y.1    Kano, Y.2    Imamoto, F.3
  • 30
    • 0028090766 scopus 로고
    • Iron requirement and search for siderophores in lactic acid bacteria
    • Pandey, A., Bringel, F. & Meyer, J. M. (1994). Iron requirement and search for siderophores in lactic acid bacteria. Appl Microbiol Biotechnol 40, 735-739.
    • (1994) Appl Microbiol Biotechnol , vol.40 , pp. 735-739
    • Pandey, A.1    Bringel, F.2    Meyer, J.M.3
  • 33
    • 0029123490 scopus 로고
    • Stress response in Lactococcus lactis: Cloning, expression analysis, and mutation of the lactococcal superoxide dismutase gene
    • Sanders, J. W., Leenhouts, K. J., Haandrikman, A. J., Venema, G. & Kok, J. (1995). Stress response in Lactococcus lactis: cloning, expression analysis, and mutation of the lactococcal superoxide dismutase gene. J Bacteriol 177, 5254-5260.
    • (1995) J Bacteriol , vol.177 , pp. 5254-5260
    • Sanders, J.W.1    Leenhouts, K.J.2    Haandrikman, A.J.3    Venema, G.4    Kok, J.5
  • 34
    • 0020398202 scopus 로고
    • Amplification and product identification of the fnr gene of Escherichia coli
    • Shaw, D. J. & Guest, J. R. (1982). Amplification and product identification of the fnr gene of Escherichia coli. J Gen Microbiol 128, 2221-2228.
    • (1982) J Gen Microbiol , vol.128 , pp. 2221-2228
    • Shaw, D.J.1    Guest, J.R.2
  • 36
    • 0028556430 scopus 로고
    • The FNR family of transcriptional regulators
    • Spiro, S. (1994). The FNR family of transcriptional regulators. Antonie Leeuwenhoek 66, 23-36.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 23-36
    • Spiro, S.1
  • 37
    • 0023571178 scopus 로고
    • Regulation and overexpression of the fnr gene of Escherichia coli
    • Spiro, S. & Guest, J. R. (1987). Regulation and overexpression of the fnr gene of Escherichia coli. J Gen Microbiol 133, 3279-3288.
    • (1987) J Gen Microbiol , vol.133 , pp. 3279-3288
    • Spiro, S.1    Guest, J.R.2
  • 38
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro, S. & Guest, J. R. (1990). FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol Rev 75, 399-428.
    • (1990) FEMS Microbiol Rev , vol.75 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 39
    • 0025173637 scopus 로고
    • Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR
    • Spiro, S., Gaston, K. L., Bell, A. I., Roberts, R. E., Busby, S. J. W. & Guest, J. R. (1990). Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR. Mol Microbiol 4, 1831-1838.
    • (1990) Mol Microbiol , vol.4 , pp. 1831-1838
    • Spiro, S.1    Gaston, K.L.2    Bell, A.I.3    Roberts, R.E.4    Busby, S.J.W.5    Guest, J.R.6
  • 40
    • 34848828105 scopus 로고
    • Accelerating effect of copper ion on the reactivation of reduced Taka-amylase A through catalysis of the oxidation of thiol groups
    • Takagi, T. & Isemura, T. (1965). Accelerating effect of copper ion on the reactivation of reduced Taka-amylase A through catalysis of the oxidation of thiol groups. J Biochem 56, 344-350.
    • (1965) J Biochem , vol.56 , pp. 344-350
    • Takagi, T.1    Isemura, T.2
  • 41
    • 0023088080 scopus 로고
    • Analysis for disulphide bonds in peptides and proteins
    • Thannhauser, T. W., Konishi, Y. & Scheraga, H. A. (1987). Analysis for disulphide bonds in peptides and proteins. Methods Enzymol 143, 115-119.
    • (1987) Methods Enzymol , vol.143 , pp. 115-119
    • Thannhauser, T.W.1    Konishi, Y.2    Scheraga, H.A.3
  • 42
    • 0015850211 scopus 로고
    • Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli
    • Thelander, L. (1973). Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli. J Biol Chem 248, 4591-4601.
    • (1973) J Biol Chem , vol.248 , pp. 4591-4601
    • Thelander, L.1
  • 43
    • 0028566977 scopus 로고
    • Oxygen-regulated gene expression in facultatively anaerobic bacteria
    • Unden, G., Becker, S., Bongaerts, J. & Six, S. (1994). Oxygen-regulated gene expression in facultatively anaerobic bacteria. Antonie Leeuwenhoek 66, 3-23.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 3-23
    • Unden, G.1    Becker, S.2    Bongaerts, J.3    Six, S.4
  • 45
    • 0001963674 scopus 로고
    • A convenient growth medium for E. coli and some other organisms
    • Vogel, H. & Bonner, D. M. (1956). A convenient growth medium for E. coli and some other organisms. Microbial Genet Bull 13, 43.
    • (1956) Microbial Genet Bull , vol.13 , pp. 43
    • Vogel, H.1    Bonner, D.M.2
  • 46
    • 0029966802 scopus 로고    scopus 로고
    • Metabolic engineering of sugar catabolism in lactic acid bacteria
    • de Vos, W. M. (1996). Metabolic engineering of sugar catabolism in lactic acid bacteria. Antonie Leeuwenhoek 70, 223-242.
    • (1996) Antonie Leeuwenhoek , vol.70 , pp. 223-242
    • De Vos, W.M.1
  • 47
    • 0023513976 scopus 로고
    • Organisation of the regulatory region of the Escherichia coli melibiose operon
    • Webster, C., Kempsall, K., Booth, I. & Busby, S. (1987). Organisation of the regulatory region of the Escherichia coli melibiose operon. Gene 59, 253-263.
    • (1987) Gene , vol.59 , pp. 253-263
    • Webster, C.1    Kempsall, K.2    Booth, I.3    Busby, S.4


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