메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

Crosstalk between ROS homeostasis and secondary metabolism in s. natalensis atcc 27448: Modulation of pimaricin production by intracellular ros

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; HYDROGEN PEROXIDE; NATAMYCIN; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; OXIDIZING AGENT;

EID: 81255195827     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027472     Document Type: Article
Times cited : (39)

References (67)
  • 1
    • 14544294545 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • Berdy J, (2005) Bioactive microbial metabolites. J Antibiot (Tokyo) 58: 1-26.
    • (2005) J Antibiot (Tokyo) , vol.58 , pp. 1-26
    • Berdy, J.1
  • 2
    • 15744383448 scopus 로고    scopus 로고
    • Regulation of secondary metabolism in streptomycetes
    • Bibb M, (2005) Regulation of secondary metabolism in streptomycetes. Current Opinion in Microbiology8: 208- 215.
    • (2005) Current Opinion in Microbiology8: , vol.208-215
    • Bibb, M.1
  • 4
    • 33745631769 scopus 로고    scopus 로고
    • Cell signaling. H2O2, a necessary evil for cell signaling
    • Rhee SG, (2006) Cell signaling. H2O2, a necessary evil for cell signaling. Science 312: 1882-1883.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 5
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G, (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 6
    • 0030936964 scopus 로고    scopus 로고
    • Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form
    • Hidalgo E, Ding H, Demple B, (1997) Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 88: 121-129.
    • (1997) Cell , vol.88 , pp. 121-129
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 7
    • 0034623713 scopus 로고    scopus 로고
    • H2O2-sensitive fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor
    • Hahn JS, Oh SY, Chater KF, Cho YH, Roe JH, (2000) H2O2-sensitive fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor. J Biol Chem 275: 38254-38260.
    • (2000) J Biol Chem , vol.275 , pp. 38254-38260
    • Hahn, J.S.1    Oh, S.Y.2    Chater, K.F.3    Cho, Y.H.4    Roe, J.H.5
  • 8
    • 0033491929 scopus 로고    scopus 로고
    • Molecular basis for enhanced biosynthesis of clavulanic acid by a redox-cycling agent, phenazine methosulfate, in Streptomyces clavuligerus
    • Kwon HJ, Kim SU, (1999) Molecular basis for enhanced biosynthesis of clavulanic acid by a redox-cycling agent, phenazine methosulfate, in Streptomyces clavuligerus. Appl Microbiol Biotechnol 53: 57-62.
    • (1999) Appl Microbiol Biotechnol , vol.53 , pp. 57-62
    • Kwon, H.J.1    Kim, S.U.2
  • 9
    • 0031963111 scopus 로고    scopus 로고
    • Enhanced biosynthesis of clavulanic acid in Streptomyces clavuligerus due to oxidative challenge by redox-cycling agents
    • Kwon HJ, Kim SU, (1998) Enhanced biosynthesis of clavulanic acid in Streptomyces clavuligerus due to oxidative challenge by redox-cycling agents. Appl Microbiol Biotechnol 49: 77-83.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 77-83
    • Kwon, H.J.1    Kim, S.U.2
  • 10
    • 0033537959 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the 26-membered ring polyene macrolide pimaricin. A new polyketide synthase organization encoded by two subclusters separated by functionalization genes
    • Aparicio JF, Colina AJ, Ceballos E, Martin JF, (1999) The biosynthetic gene cluster for the 26-membered ring polyene macrolide pimaricin. A new polyketide synthase organization encoded by two subclusters separated by functionalization genes. J Biol Chem 274: 10133-10139.
    • (1999) J Biol Chem , vol.274 , pp. 10133-10139
    • Aparicio, J.F.1    Colina, A.J.2    Ceballos, E.3    Martin, J.F.4
  • 12
    • 64049085732 scopus 로고    scopus 로고
    • Enzymology of the polyenes pimaricin and candicidin biosynthesis
    • Martin JF, Aparicio JF, (2009) Enzymology of the polyenes pimaricin and candicidin biosynthesis. Methods Enzymol 459: 215-242.
    • (2009) Methods Enzymol , vol.459 , pp. 215-242
    • Martin, J.F.1    Aparicio, J.F.2
  • 13
    • 1942539982 scopus 로고    scopus 로고
    • Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis
    • Anton N, Mendes MV, Martin JF, Aparicio JF, (2004) Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis. J Bacteriol 186: 2567-2575.
    • (2004) J Bacteriol , vol.186 , pp. 2567-2575
    • Anton, N.1    Mendes, M.V.2    Martin, J.F.3    Aparicio, J.F.4
  • 14
    • 34948839957 scopus 로고    scopus 로고
    • PimM, a PAS domain positive regulator of pimaricin biosynthesis in Streptomyces natalensis
    • Anton N, Santos-Aberturas J, Mendes MV, Guerra SM, Martin JF, et al. (2007) PimM, a PAS domain positive regulator of pimaricin biosynthesis in Streptomyces natalensis. Microbiology153: 3174-3183.
    • (2007) Microbiology , vol.153 , pp. 3174-3183
    • Anton, N.1    Santos-Aberturas, J.2    Mendes, M.V.3    Guerra, S.M.4    Martin, J.F.5
  • 15
    • 33947265302 scopus 로고    scopus 로고
    • Cholesterol oxidases act as signaling proteins for the biosynthesis of the polyene macrolide pimaricin
    • Mendes MV, Recio E, Anton N, Guerra SM, Santos-Aberturas J, et al. (2007) Cholesterol oxidases act as signaling proteins for the biosynthesis of the polyene macrolide pimaricin. Chem Biol 14: 279-290.
    • (2007) Chem Biol , vol.14 , pp. 279-290
    • Mendes, M.V.1    Recio, E.2    Anton, N.3    Guerra, S.M.4    Santos-Aberturas, J.5
  • 16
    • 0034945645 scopus 로고    scopus 로고
    • Engineered biosynthesis of novel polyenes: a pimaricin derivative produced by targeted gene disruption in Streptomyces natalensis
    • Mendes MV, Recio E, Fouces R, Luiten R, Martin JF, et al. (2001) Engineered biosynthesis of novel polyenes: a pimaricin derivative produced by targeted gene disruption in Streptomyces natalensis. Chem Biol 8: 635-644.
    • (2001) Chem Biol , vol.8 , pp. 635-644
    • Mendes, M.V.1    Recio, E.2    Fouces, R.3    Luiten, R.4    Martin, J.F.5
  • 17
    • 67749142402 scopus 로고    scopus 로고
    • PimT, an amino acid exporter controls polyene production via secretion of the quorum sensing pimaricin-inducer PI-factor in Streptomyces natalensis
    • Vicente CM, Santos-Aberturas J, Guerra SM, Payero TD, Martin JF, et al. (2009) PimT, an amino acid exporter controls polyene production via secretion of the quorum sensing pimaricin-inducer PI-factor in Streptomyces natalensis. Microb Cell Fact 8: 33.
    • (2009) Microb Cell Fact , vol.8 , pp. 33
    • Vicente, C.M.1    Santos-Aberturas, J.2    Guerra, S.M.3    Payero, T.D.4    Martin, J.F.5
  • 18
    • 0033763409 scopus 로고    scopus 로고
    • A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis
    • Aparicio JF, Fouces R, Mendes MV, Olivera N, Martin JF, (2000) A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis. Chem Biol 7: 895-905.
    • (2000) Chem Biol , vol.7 , pp. 895-905
    • Aparicio, J.F.1    Fouces, R.2    Mendes, M.V.3    Olivera, N.4    Martin, J.F.5
  • 19
    • 79953201151 scopus 로고    scopus 로고
    • Molecular control of polyene macrolide biosynthesis: direct binding of the regulator PimM to eight promoters of pimaricin genes and identification of binding boxes
    • Santos-Aberturas J, Vicente CM, Guerra SM, Payero TD, Martin JF, et al. (2011) Molecular control of polyene macrolide biosynthesis: direct binding of the regulator PimM to eight promoters of pimaricin genes and identification of binding boxes. The Journal of biological chemistry 286: 9150-9161.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 9150-9161
    • Santos-Aberturas, J.1    Vicente, C.M.2    Guerra, S.M.3    Payero, T.D.4    Martin, J.F.5
  • 20
    • 33847661977 scopus 로고    scopus 로고
    • The two-component phoR-phoP system of Streptomyces natalensis: Inactivation or deletion of phoP reduces the negative phosphate regulation of pimaricin biosynthesis
    • Mendes MV, Tunca S, Anton N, Recio E, Sola-Landa A, et al. (2007) The two-component phoR-phoP system of Streptomyces natalensis: Inactivation or deletion of phoP reduces the negative phosphate regulation of pimaricin biosynthesis. Metab Eng 9: 217-227.
    • (2007) Metab Eng , vol.9 , pp. 217-227
    • Mendes, M.V.1    Tunca, S.2    Anton, N.3    Recio, E.4    Sola-Landa, A.5
  • 21
    • 0029047507 scopus 로고
    • Developmental control of the heat-shock stress regulon in Streptomyces coelicolor
    • Puglia AM, Vohradsky J, Thompson CJ, (1995) Developmental control of the heat-shock stress regulon in Streptomyces coelicolor. Mol Microbiol 17: 737-746.
    • (1995) Mol Microbiol , vol.17 , pp. 737-746
    • Puglia, A.M.1    Vohradsky, J.2    Thompson, C.J.3
  • 22
    • 0035576880 scopus 로고    scopus 로고
    • Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA microarrays
    • Huang J, Lih CJ, Pan KH, Cohen SN, (2001) Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA microarrays. Genes Dev 15: 3183-3192.
    • (2001) Genes Dev , vol.15 , pp. 3183-3192
    • Huang, J.1    Lih, C.J.2    Pan, K.H.3    Cohen, S.N.4
  • 23
    • 77349116867 scopus 로고    scopus 로고
    • The dynamic architecture of the metabolic switch in Streptomyces coelicolor
    • Nieselt K, Battke F, Herbig A, Bruheim P, Wentzel A, et al. (2010) The dynamic architecture of the metabolic switch in Streptomyces coelicolor. BMC Genomics 11: 10.
    • (2010) BMC Genomics , vol.11 , pp. 10
    • Nieselt, K.1    Battke, F.2    Herbig, A.3    Bruheim, P.4    Wentzel, A.5
  • 24
    • 0030911601 scopus 로고    scopus 로고
    • Isolation and expression of the catA gene encoding the major vegetative catalase in Streptomyces coelicolor Muller
    • Cho YH, Roe JH, (1997) Isolation and expression of the catA gene encoding the major vegetative catalase in Streptomyces coelicolor Muller. J Bacteriol 179: 4049-4052.
    • (1997) J Bacteriol , vol.179 , pp. 4049-4052
    • Cho, Y.H.1    Roe, J.H.2
  • 26
    • 0033026250 scopus 로고    scopus 로고
    • The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS
    • Zou P, Borovok I, Ortiz de Orue Lucana D, Muller D, Schrempf H, (1999) The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS. Microbiology145: 549-559.
    • (1999) Microbiology , vol.145 , pp. 549-559
    • Zou, P.1    Borovok, I.2    Ortiz de Orue Lucana, D.3    Muller, D.4    Schrempf, H.5
  • 27
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coli
    • Seaver LC, Imlay JA, (2001) Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coli. J Bacteriol 183: 7173-7181.
    • (2001) J Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 28
    • 33645037891 scopus 로고    scopus 로고
    • The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
    • Lee JW, Helmann JD, (2006) The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Nature 440: 363-367.
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 29
    • 33747722767 scopus 로고    scopus 로고
    • Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR
    • Lee JW, Helmann JD, (2006) Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR. J Biol Chem 281: 23567-23578.
    • (2006) J Biol Chem , vol.281 , pp. 23567-23578
    • Lee, J.W.1    Helmann, J.D.2
  • 30
    • 0023945399 scopus 로고
    • Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures
    • Parker MW, Blake CC, (1988) Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett 229: 377-382.
    • (1988) FEBS Lett , vol.229 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.2
  • 31
    • 0022407817 scopus 로고
    • The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4-A resolution
    • Stallings WC, Pattridge KA, Strong RK, Ludwig ML, (1985) The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4-A resolution. J Biol Chem 260: 16424-16432.
    • (1985) J Biol Chem , vol.260 , pp. 16424-16432
    • Stallings, W.C.1    Pattridge, K.A.2    Strong, R.K.3    Ludwig, M.L.4
  • 32
    • 0034618681 scopus 로고    scopus 로고
    • Identification of cis site involved in nickel-responsive transcriptional repression of sodF gene coding for Fe- and Zn-containing superoxide dismutase of Streptomyces griseus
    • Kim JS, Jang JH, Lee JW, Kang SO, Kim KS, et al. (2000) Identification of cis site involved in nickel-responsive transcriptional repression of sodF gene coding for Fe- and Zn-containing superoxide dismutase of Streptomyces griseus. Biochim Biophys Acta 1493: 200-207.
    • (2000) Biochim Biophys Acta , vol.1493 , pp. 200-207
    • Kim, J.S.1    Jang, J.H.2    Lee, J.W.3    Kang, S.O.4    Kim, K.S.5
  • 34
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust B, Challis GL, Fowler K, Kieser T, Chater KF, (2003) PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc Natl Acad Sci U S A 100: 1541-1546.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 35
    • 33645231502 scopus 로고    scopus 로고
    • An efficient gene transfer system for the pimaricin producer Streptomyces natalensis
    • Enriquez LL, Mendes MV, Anton N, Tunca S, Guerra SM, et al. (2006) An efficient gene transfer system for the pimaricin producer Streptomyces natalensis. FEMS Microbiol Lett 257: 312-318.
    • (2006) FEMS Microbiol Lett , vol.257 , pp. 312-318
    • Enriquez, L.L.1    Mendes, M.V.2    Anton, N.3    Tunca, S.4    Guerra, S.M.5
  • 36
    • 0034487106 scopus 로고    scopus 로고
    • Influence of inoculum type and cultivation conditions on natamycin production by Streptomyces natalensis
    • el-Enshasy HA, Farid MA, el-Sayed el SA, (2000) Influence of inoculum type and cultivation conditions on natamycin production by Streptomyces natalensis. J Basic Microbiol 40: 333-342.
    • (2000) J Basic Microbiol , vol.40 , pp. 333-342
    • el-Enshasy, H.A.1    Farid, M.A.2    el-Sayed el, S.A.3
  • 37
    • 0033971399 scopus 로고    scopus 로고
    • A developmentally regulated catalase required for proper differentiation and osmoprotection of Streptomyces coelicolor
    • Cho YH, Lee EJ, Roe JH, (2000) A developmentally regulated catalase required for proper differentiation and osmoprotection of Streptomyces coelicolor. Mol Microbiol 35: 150-160.
    • (2000) Mol Microbiol , vol.35 , pp. 150-160
    • Cho, Y.H.1    Lee, E.J.2    Roe, J.H.3
  • 38
    • 0033614461 scopus 로고    scopus 로고
    • Duplicate genes for Fe-containing superoxide dismutase in Streptomyces coelicolor A3(2)
    • Chung HJ, Kim EJ, Suh B, Choi JH, Roe JH, (1999) Duplicate genes for Fe-containing superoxide dismutase in Streptomyces coelicolor A3(2). Gene 231: 87-93.
    • (1999) Gene , vol.231 , pp. 87-93
    • Chung, H.J.1    Kim, E.J.2    Suh, B.3    Choi, J.H.4    Roe, J.H.5
  • 39
    • 0029849183 scopus 로고    scopus 로고
    • Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
    • Kim FJ, Kim HP, Hah YC, Roe JH, (1996) Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor. Eur J Biochem 241: 178-185.
    • (1996) Eur J Biochem , vol.241 , pp. 178-185
    • Kim, F.J.1    Kim, H.P.2    Hah, Y.C.3    Roe, J.H.4
  • 40
    • 0031922352 scopus 로고    scopus 로고
    • Expression and regulation of the sodF gene encoding iron- and zinc-containing superoxide dismutase in Streptomyces coelicolor Muller
    • Kim EJ, Chung HJ, Suh B, Hah YC, Roe JH, (1998) Expression and regulation of the sodF gene encoding iron- and zinc-containing superoxide dismutase in Streptomyces coelicolor Muller. J Bacteriol 180: 2014-2020.
    • (1998) J Bacteriol , vol.180 , pp. 2014-2020
    • Kim, E.J.1    Chung, H.J.2    Suh, B.3    Hah, Y.C.4    Roe, J.H.5
  • 41
    • 0028588511 scopus 로고
    • Characterization of the major catalase from Streptomyces coelicolor ATCC 10147
    • Kim H, Lee JS, Hah YC, Roe JH, (1994) Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. Microbiology140 (Pt 12): 3391-3397.
    • (1994) Microbiology , vol.140 , Issue.PART 12 , pp. 3391-3397
    • Kim, H.1    Lee, J.S.2    Hah, Y.C.3    Roe, J.H.4
  • 42
    • 0036778158 scopus 로고    scopus 로고
    • Role of OxyR as a peroxide-sensing positive regulator in Streptomyces coelicolor A3(2)
    • Hahn JS, Oh SY, Roe JH, (2002) Role of OxyR as a peroxide-sensing positive regulator in Streptomyces coelicolor A3(2). J Bacteriol 184: 5214-5222.
    • (2002) J Bacteriol , vol.184 , pp. 5214-5222
    • Hahn, J.S.1    Oh, S.Y.2    Roe, J.H.3
  • 43
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • Forman HJ, Maiorino M, Ursini F, (2010) Signaling functions of reactive oxygen species. Biochemistry 49: 835-842.
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 45
    • 79958026489 scopus 로고    scopus 로고
    • Superoxide dismutase (SOD) genes in Streptomyces peucetius: Effects of SODs on secondary metabolites production
    • Kanth BK, Jnawali HN, Niraula NP, Sohng JK, (2010) Superoxide dismutase (SOD) genes in Streptomyces peucetius: Effects of SODs on secondary metabolites production. Microbiol Res.
    • (2010) Microbiol Res
    • Kanth, B.K.1    Jnawali, H.N.2    Niraula, N.P.3    Sohng, J.K.4
  • 46
    • 0034460324 scopus 로고    scopus 로고
    • A Xanthomonas alkyl hydroperoxide reductase subunit C (ahpC) mutant showed an altered peroxide stress response and complex regulation of the compensatory response of peroxide detoxification enzymes
    • Mongkolsuk S, Whangsuk W, Vattanaviboon P, Loprasert S, Fuangthong M, (2000) A Xanthomonas alkyl hydroperoxide reductase subunit C (ahpC) mutant showed an altered peroxide stress response and complex regulation of the compensatory response of peroxide detoxification enzymes. J Bacteriol 182: 6845-6849.
    • (2000) J Bacteriol , vol.182 , pp. 6845-6849
    • Mongkolsuk, S.1    Whangsuk, W.2    Vattanaviboon, P.3    Loprasert, S.4    Fuangthong, M.5
  • 47
    • 33846561089 scopus 로고    scopus 로고
    • Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus
    • Cosgrove K, Coutts G, Jonsson IM, Tarkowski A, Kokai-Kun JF, et al. (2007) Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus. J Bacteriol 189: 1025-1035.
    • (2007) J Bacteriol , vol.189 , pp. 1025-1035
    • Cosgrove, K.1    Coutts, G.2    Jonsson, I.M.3    Tarkowski, A.4    Kokai-Kun, J.F.5
  • 48
    • 0035195997 scopus 로고    scopus 로고
    • Regulation of sporulation in Streptomyces coelicolor A3(2): a checkpoint multiplex?
    • Chater KF, (2001) Regulation of sporulation in Streptomyces coelicolor A3(2): a checkpoint multiplex? Current Opinion in Microbiology4: 667-673.
    • (2001) Current Opinion in Microbiology , vol.4 , pp. 667-673
    • Chater, K.F.1
  • 49
    • 0033118280 scopus 로고    scopus 로고
    • Starvation, cessation of growth and bacterial aging
    • Nystrom T, (1999) Starvation, cessation of growth and bacterial aging. Current Opinion in Microbiology2: 214-219.
    • (1999) Current Opinion in Microbiology , vol.2 , pp. 214-219
    • Nystrom, T.1
  • 50
    • 33845566494 scopus 로고    scopus 로고
    • Effects of dissolved oxygen level on avermectin B-1a production by Streptomyces avermitilis in computer-controlled bioreactor cultures
    • Song SK, Jeong YS, Kim PH, Chun GT, (2006) Effects of dissolved oxygen level on avermectin B-1a production by Streptomyces avermitilis in computer-controlled bioreactor cultures. Journal of Microbiologyand Biotechnology 16: 1690-1698.
    • (2006) Journal of Microbiologyand Biotechnology , vol.16 , pp. 1690-1698
    • Song, S.K.1    Jeong, Y.S.2    Kim, P.H.3    Chun, G.T.4
  • 51
    • 0026158428 scopus 로고
    • Effect of dissolved oxygen control on growth and antibiotic production in Streptomyces clavuligerus fermentations
    • Yegneswaran PK, Gray MR, Thompson BG, (1991) Effect of dissolved oxygen control on growth and antibiotic production in Streptomyces clavuligerus fermentations. Biotechnol Prog 7: 246-250.
    • (1991) Biotechnol Prog , vol.7 , pp. 246-250
    • Yegneswaran, P.K.1    Gray, M.R.2    Thompson, B.G.3
  • 54
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers RF Jr, Sizer IW, (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133-140.
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers Jr., R.F.1    Sizer, I.W.2
  • 55
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I, (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44: 276-287.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 56
    • 0021139249 scopus 로고
    • Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase
    • Clare DA, Duong MN, Darr D, Archibald F, Fridovich I, (1984) Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem 140: 532-537.
    • (1984) Anal Biochem , vol.140 , pp. 532-537
    • Clare, D.A.1    Duong, M.N.2    Darr, D.3    Archibald, F.4    Fridovich, I.5
  • 57
    • 0026088567 scopus 로고
    • Chromogenic substrates for horseradish peroxidase
    • Conyers SM, Kidwell DA, (1991) Chromogenic substrates for horseradish peroxidase. Anal Biochem 192: 207-211.
    • (1991) Anal Biochem , vol.192 , pp. 207-211
    • Conyers, S.M.1    Kidwell, D.A.2
  • 58
    • 0021827654 scopus 로고
    • Bacteriocuprein superoxide dismutases in pseudomonads
    • Steinman HM, (1985) Bacteriocuprein superoxide dismutases in pseudomonads. J Bacteriol 162: 1255-1260.
    • (1985) J Bacteriol , vol.162 , pp. 1255-1260
    • Steinman, H.M.1
  • 59
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg A, Obermaier C, Boguth G, Harder A, Scheibe B, et al. (2000) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 21: 1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Gorg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4    Scheibe, B.5
  • 60
    • 84884843098 scopus 로고    scopus 로고
    • Protein Detection in Gels by Silver Staining: A Procedure Compatible with Mass Spectrometry
    • In: Celis JE, Carter N, Simons K, Small J, Hunter T, editors, Elsevier Academic Press
    • Gromova I, Celis JE, Protein Detection in Gels by Silver Staining: A Procedure Compatible with Mass Spectrometry. In: Celis JE, Carter N, Simons K, Small J, Hunter T, editors. (2006) Cell Biology: A Laboratory Handbook. 3rd ed Elsevier Academic Press pp. 219-223.
    • (2006) Cell Biology: A Laboratory Handbook , pp. 219-223
    • Gromova, I.1    Celis, J.E.2
  • 61
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW, (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 63
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D, (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 64
    • 0026575735 scopus 로고
    • Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector
    • MacNeil DJ, Gewain KM, Ruby CL, Dezeny G, Gibbons PH, et al. (1992) Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector. Gene 111: 61-68.
    • (1992) Gene , vol.111 , pp. 61-68
    • MacNeil, D.J.1    Gewain, K.M.2    Ruby, C.L.3    Dezeny, G.4    Gibbons, P.H.5
  • 65
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 66
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov PP, Wackernagel W, (1995) Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158: 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 67
    • 0032898961 scopus 로고    scopus 로고
    • Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2)
    • Paget MS, Chamberlin L, Atrih A, Foster SJ, Buttner MJ, (1999) Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2). J Bacteriol 181: 204-211.
    • (1999) J Bacteriol , vol.181 , pp. 204-211
    • Paget, M.S.1    Chamberlin, L.2    Atrih, A.3    Foster, S.J.4    Buttner, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.