메뉴 건너뛰기




Volumn 37, Issue 4, 2009, Pages 681-691

The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase sens in a redox-dependent manner

Author keywords

Heme binding protein HbpS; Redox stress; Streptomyces; Two component system SenS SenR

Indexed keywords

HBPS PROTEIN; HEMOPROTEIN; IRON; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG;

EID: 70349584359     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-008-0188-5     Document Type: Article
Times cited : (14)

References (44)
  • 2
    • 0027536224 scopus 로고
    • Mode of action of three endo-beta-1, 4-xylanases of Streptomyces lividans
    • 8457588 1:CAS:528:DyaK3sXltlCiu7k%3D
    • P Biely D Kluepfel R Morosoli F Shareck 1993 Mode of action of three endo-beta-1, 4-xylanases of Streptomyces lividans Biochim Biophys Acta 1162 246 254 8457588 1:CAS:528:DyaK3sXltlCiu7k%3D
    • (1993) Biochim Biophys Acta , vol.1162 , pp. 246-254
    • Biely, P.1    Kluepfel, D.2    Morosoli, R.3    Shareck, F.4
  • 3
    • 34447632499 scopus 로고    scopus 로고
    • DNA-binding characteristics of the regulator SenR in response to phosphorylation by the sensor histidine autokinase SenS from Streptomyces reticuli
    • DOI 10.1111/j.1742-4658.2007.05923.x
    • G Bogel H Schrempf D Ortiz de Orué Lucana 2007 DNA-binding characteristics of the regulator SenR in response to phosphorylation by the sensor histidine autokinase SenS from Streptomyces reticuli FEBS J 274 3900 3913 10.1111/j.1742-4658.2007.05923.x 17617222 10.1111/j.1742-4658.2007.05923.x 1:CAS:528:DC%2BD2sXptFCnur4%3D (Pubitemid 47087678)
    • (2007) FEBS Journal , vol.274 , Issue.15 , pp. 3900-3913
    • Bogel, G.1    Schrempf, H.2    Ortiz De Orue Lucana, D.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of the protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • MM Bradford 1976 A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of the protein-dye binding Anal Biochem 72 248 254 10.1016/0003-2697(76)90527-3 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0025239795 scopus 로고
    • The physiological role of zinc as an antioxidant
    • DOI 10.1016/0891-5849(90)90076-U
    • TM Bray WJ Bettger 1990 The physiological role of zinc as an antioxidant Free Radic Biol Med 8 281 291 10.1016/0891-5849(90)90076-U 2187766 10.1016/0891-5849(90)90076-U 1:CAS:528:DyaK3MXks1yqtbg%3D (Pubitemid 20137051)
    • (1990) Free Radical Biology and Medicine , vol.8 , Issue.3 , pp. 281-291
    • Bray, T.M.1    Bettger, W.J.2
  • 6
    • 34548787792 scopus 로고    scopus 로고
    • Reactive oxygen species and cellular oxygen sensing
    • DOI 10.1016/j.freeradbiomed.2007.07.001, PII S0891584907004637
    • TP Cash Y Pan MC Simon 2007 Reactive oxygen species and cellular oxygen sensing Free Radic Biol Med 43 1219 1225 10.1016/j.freeradbiomed.2007.07.001 17893032 10.1016/j.freeradbiomed.2007.07.001 1:CAS:528:DC%2BD2sXhtVOis7nP (Pubitemid 47429935)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.9 , pp. 1219-1225
    • Cash, T.P.1    Pan, Y.2    Simon, M.C.3
  • 7
    • 0036372533 scopus 로고    scopus 로고
    • Fe(III)-mediated cellular toxicity
    • DOI 10.1046/j.1365-2958.2002.03041.x
    • S Chamnongpol W Dodson MJ Cromie ZL Harris EA Groisman 2002 Fe(III)-mediated cellular toxicity Mol Microbiol 45 711 719 10.1046/j.1365-2958. 2002.03041.x 12139617 10.1046/j.1365-2958.2002.03041.x 1:CAS:528: DC%2BD38Xmt1yrtr0%3D (Pubitemid 34989178)
    • (2002) Molecular Microbiology , vol.45 , Issue.3 , pp. 711-719
    • Chamnongpol, S.1    Dodson, W.2    Cromie, M.J.3    Harris, Z.L.4    Groisman, E.A.5
  • 8
    • 30844444172 scopus 로고    scopus 로고
    • Bacterial tyrosinases
    • DOI 10.1016/j.syapm.2005.07.012, PII S0723202005001438
    • H Claus H Decker 2006 Bacterial tyrosinases Syst Appl Microbiol 29 3 14 10.1016/j.syapm.2005.07.012 16423650 10.1016/j.syapm.2005.07.012 1:CAS:528:DC%2BD28Xjt1Krs7s%3D (Pubitemid 43102498)
    • (2006) Systematic and Applied Microbiology , vol.29 , Issue.1 , pp. 3-14
    • Claus, H.1    Decker, H.2
  • 10
    • 34547151297 scopus 로고    scopus 로고
    • The VicRK system of Streptococcus mutans responds to oxidative stress
    • 17586705 10.1177/154405910708600705 1:CAS:528:DC%2BD2sXot1antLY%3D
    • DM Deng MJ Liu JM ten Cate W Crielaard 2007 The VicRK system of Streptococcus mutans responds to oxidative stress J Dent Res 86 606 610 17586705 10.1177/154405910708600705 1:CAS:528:DC%2BD2sXot1antLY%3D
    • (2007) J Dent Res , vol.86 , pp. 606-610
    • Deng, D.M.1    Liu, M.J.2    Ten Cate, J.M.3    Crielaard, W.4
  • 11
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • DOI 10.1128/JB.185.8.2432-2440.2003
    • PA DiGiuseppe TJ Silhavy 2003 Signal detection and target gene induction by the CpxRA two-component system J Bacteriol 185 2432 2440 10.1128/JB.185.8. 2432-2440.2003 12670966 10.1128/JB.185.8.2432-2440.2003 1:CAS:528: DC%2BD3sXivFKrsrg%3D (Pubitemid 36417966)
    • (2003) Journal of Bacteriology , vol.185 , Issue.8 , pp. 2432-2440
    • DiGiuseppe, P.A.1    Silhavy, T.J.2
  • 12
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • 10.1093/nar/16.13.6127 3041370 10.1093/nar/16.13.6127 1:CAS:528:DyaL1cXltVGrtLw%3D
    • WJ Dower JF Miller CW Ragsdale 1988 High efficiency transformation of E. coli by high voltage electroporation Nucleic Acids Res 16 6127 6145 10.1093/nar/16.13.6127 3041370 10.1093/nar/16.13.6127 1:CAS:528: DyaL1cXltVGrtLw%3D
    • (1988) Nucleic Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 13
    • 0344666703 scopus 로고    scopus 로고
    • 2 Sensor HupUV and the Histidine Kinase HupT Controls HupSL Hydrogenase Synthesis in Rhodobacter capsulatus
    • DOI 10.1128/JB.185.24.7111-7119.2003
    • S Elsen O Dúche A Colbeau 2003 Interaction between the sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus J Bacteriol 185 7111 7119 10.1128/JB.185.24.7111-7119. 2003 14645270 10.1128/JB.185.24.7111-7119.2003 1:CAS:528:DC%2BD3sXpvVaqsLg%3D (Pubitemid 37509826)
    • (2003) Journal of Bacteriology , vol.185 , Issue.24 , pp. 7111-7119
    • Elsen, S.1    Duche, O.2    Colbeau, A.3
  • 14
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in the presence of iron
    • HJH Fenton 1986 Oxidation of tartaric acid in the presence of iron J Chem Soc 65 899 910
    • (1986) J Chem Soc , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 15
    • 39749110624 scopus 로고    scopus 로고
    • Oxidative stress and iron homeostasis: Mechanistic and health aspects
    • DOI 10.1080/10408360701713104, PII 790776652
    • D Galaris K Pantopoulos 2008 Oxidative stress and iron homoeostasis: mechanistic and health aspects Crit Rev Clin Lab Sci 45 1 23 10.1080/10408360701713104 18293179 10.1080/10408360701713104 1:CAS:528:DC%2BD1cXit1Cksrk%3D (Pubitemid 351299652)
    • (2008) Critical Reviews in Clinical Laboratory Sciences , vol.45 , Issue.1 , pp. 1-23
    • Galaris, D.1    Pantopoulos, K.2
  • 16
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • 10.1074/jbc.270.23.13681 10.1074/jbc.270.23.13681
    • B Gonzales-Flecha B Demple 1995 Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli J Biol Chem 270 13681 13687 10.1074/jbc.270.23.13681 10.1074/jbc.270.23.13681
    • (1995) J Biol Chem , vol.270 , pp. 13681-13687
    • Gonzales-Flecha, B.1    Demple, B.2
  • 17
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • DOI 10.1128/JB.183.17.4941-4949.2001
    • JA Hoch KI Varughese 2001 Keeping signals straight in phosphorelay signal transduction J Bacteriol 183 4941 4949 10.1128/JB.183.17.4941-4949.2001 11489844 10.1128/JB.183.17.4941-4949.2001 1:CAS:528:DC%2BD3MXmtFKku7o%3D (Pubitemid 32750919)
    • (2001) Journal of Bacteriology , vol.183 , Issue.17 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 20
    • 4844230017 scopus 로고    scopus 로고
    • Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2)
    • DOI 10.1099/mic.0.27181-0
    • MI Hutchings PA Hoskisson G Chandra MJ Buttner 2004 Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2) Microbiology 150 2795 2806 10.1099/mic.0.27181-0 15347739 10.1099/mic.0.27181-0 1:CAS:528: DC%2BD2cXotF2js78%3D (Pubitemid 39317782)
    • (2004) Microbiology , vol.150 , Issue.9 , pp. 2795-2806
    • Hutchings, M.I.1    Hoskisson, P.A.2    Chandra, G.3    Buttner, M.J.4
  • 21
    • 34147117736 scopus 로고    scopus 로고
    • DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis
    • DOI 10.1021/bi602422p
    • A Ioanoviciu ET Yukl P Moënne-Loccoz PR de Montellano 2007 DevS, a heme-containing two-component sensor of Mycobacterium tuberculosis Biochemistry 46 4250 4260 10.1021/bi602422p 17371046 10.1021/bi602422p 1:CAS:528: DC%2BD2sXjtFKlu7c%3D (Pubitemid 46559392)
    • (2007) Biochemistry , vol.46 , Issue.14 , pp. 4250-4260
    • Ioanovichi, A.1    Yukl, E.T.2    Moenne-Loccoz, P.3    Ortiz De Montellano, P.R.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • 10.1038/227680a0 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of the bacteriophage T4 Nature 227 680 685 10.1038/227680a0 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two component signal transduction pathways
    • 10.1146/annurev.genet.41.042007.170548 18076326 10.1146/annurev.genet.41. 042007.170548 1:CAS:528:DC%2BD1cXns1SjsQ%3D%3D
    • MT Laub M Goulian 2007 Specificity in two component signal transduction pathways Annu Rev Genet 41 121 145 10.1146/annurev.genet.41.042007.170548 18076326 10.1146/annurev.genet.41.042007.170548 1:CAS:528:DC%2BD1cXns1SjsQ%3D%3D
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 24
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • 10.1016/S0076-6879(57)03413-8 10.1016/S0076-6879(57)03413-8
    • E Layne 1957 Spectrophotometric and turbidimetric methods for measuring proteins Methods Enzymol 3 447 455 10.1016/S0076-6879(57)03413-8 10.1016/S0076-6879(57)03413-8
    • (1957) Methods Enzymol , vol.3 , pp. 447-455
    • Layne, E.1
  • 25
    • 0032835113 scopus 로고    scopus 로고
    • Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: Nitrate elicits a superior anion ligand response compared to nitrite
    • 10464202 1:CAS:528:DyaK1MXlvVSlsLc%3D
    • AI Lee A Delgado RP Gunsalus 1999 Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: nitrate elicits a superior anion ligand response compared to nitrite J Bacteriol 181 5309 5316 10464202 1:CAS:528:DyaK1MXlvVSlsLc%3D
    • (1999) J Bacteriol , vol.181 , pp. 5309-5316
    • Lee, A.I.1    Delgado, A.2    Gunsalus, R.P.3
  • 26
    • 0021076584 scopus 로고
    • Lambda charon vectors (Ch32, 33, 34 and 35) adapted for DNA cloning in recombinant-deficient hosts
    • 10.1016/0378-1119(83)90187-7 6323258 10.1016/0378-1119(83)90187-7 1:CAS:528:DyaL2cXhsFWqsLY%3D
    • WA Loenen FR Blattner 1983 Lambda charon vectors (Ch32, 33, 34 and 35) adapted for DNA cloning in recombinant-deficient hosts Gene 26 171 179 10.1016/0378-1119(83)90187-7 6323258 10.1016/0378-1119(83)90187-7 1:CAS:528:DyaL2cXhsFWqsLY%3D
    • (1983) Gene , vol.26 , pp. 171-179
    • Loenen, W.A.1    Blattner, F.R.2
  • 28
    • 4444235114 scopus 로고    scopus 로고
    • The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB
    • 10.1099/mic.0.27091-0 15289554 10.1099/mic.0.27091-0
    • Dortiz de Orué Lucana T Schaa H Schrempf 2004 The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB Microbiology 150 2575 2585 10.1099/mic.0.27091-0 15289554 10.1099/mic.0.27091-0
    • (2004) Microbiology , vol.150 , pp. 2575-2585
    • De Orué Lucana, D.1    Schaa, T.2    Schrempf, H.3
  • 29
    • 0033764027 scopus 로고    scopus 로고
    • The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues
    • 10.1007/s004380000328 11085275 10.1007/s004380000328
    • D Ortiz de Orué Lucana H Schrempf 2000 The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues Mol Gen Genet 264 341 353 10.1007/s004380000328 11085275 10.1007/s004380000328
    • (2000) Mol Gen Genet , vol.264 , pp. 341-353
    • Lucana Orué De D.Ortiz1    Schrempf, H.2
  • 30
    • 27844486088 scopus 로고    scopus 로고
    • Identification of a novel two-component system SenS/SenR modulating the production of the catalase-peroxidase CpeB and the haem-binding protein HbpS in Streptomyces reticuli
    • DOI 10.1099/mic.0.28298-0
    • D Ortiz de Orué Lucana P Zou M Nierhaus H Schrempf 2005 Identification of a novel two-component system SenS/SenR modulating the production of the catalase-peroxidase CpeB and the haem-binding protein HbpS in Streptomyces reticuli Microbiology 151 3603 3614 10.1099/mic.0.28298-0 16272382 10.1099/mic.0.28298-0 (Pubitemid 41637705)
    • (2005) Microbiology , vol.151 , Issue.11 , pp. 3603-3614
    • De Orue Lucana, D.O.1    Zou, P.2    Nierhaus, M.3    Schrempf, H.4
  • 32
    • 47249120854 scopus 로고    scopus 로고
    • The PhoQ histidine kinases of Salmonella and Pseudomonas spp. are structurally and functionally different: Evidence that pH and antimicrobial peptide sensing contribute to mammalian pathogenesis
    • DOI 10.1111/j.1365-2958.2008.06303.x
    • LR Prost ME Daley MW Bader RE Klevit SI Miller 2008 The PhoQ histidine kinases of Salmonella and Pseudomonas spp. are structurally and functionally different: evidence that pH and antimicrobial peptide sensing contribute to mammalian pathogenesis Mol Microbiol 69 503 519 10.1111/j.1365-2958.2008.06303.x 18532985 10.1111/j.1365-2958.2008.06303.x 1:CAS:528:DC%2BD1cXoslyjt78%3D (Pubitemid 351988020)
    • (2008) Molecular Microbiology , vol.69 , Issue.2 , pp. 503-519
    • Prost, L.R.1    Daley, M.E.2    Bader, M.W.3    Klevit, R.E.4    Miller, S.I.5
  • 34
    • 0032833084 scopus 로고    scopus 로고
    • Identification of a two-component signal transduction system from Corynebacterium diphteriae that activates gene expression in response to the presence of heme and hemoglobin
    • 10464204 1:CAS:528:DyaK1MXlvVSlsb8%3D
    • MP Schmitt 1999 Identification of a two-component signal transduction system from Corynebacterium diphteriae that activates gene expression in response to the presence of heme and hemoglobin J Bacteriol 181 5330 5340 10464204 1:CAS:528:DyaK1MXlvVSlsb8%3D
    • (1999) J Bacteriol , vol.181 , pp. 5330-5340
    • Schmitt, M.P.1
  • 35
    • 0034669693 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion
    • DOI 10.1016/S0891-5849(00)00432-9, PII S0891584900004329
    • KK Singh 2000 The Saccharomyces cerevisae Sln1-Ssk1p two-component system mediates response to oxidative stress and in an oxygen dependent fashion Free Radic Biol Med 29 1043 1050 10.1016/S0891-5849(00)00432-9 11084293 10.1016/S0891-5849(00)00432-9 1:CAS:528:DC%2BD3cXotVCru7w%3D (Pubitemid 30838826)
    • (2000) Free Radical Biology and Medicine , vol.29 , Issue.10 , pp. 1043-1050
    • Singh, K.K.1
  • 36
    • 34548857623 scopus 로고    scopus 로고
    • Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing
    • DOI 10.1074/jbc.M703797200
    • DL Stauff VJ Torres EP Skaar 2007 Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing J Biol Chem 282 36 26111 26121 10.1074/jbc.M703797200 17635909 10.1074/jbc.M703797200 1:CAS:528:DC%2BD2sXpslGjsLk%3D (Pubitemid 47443805)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26111-26121
    • Stauff, D.L.1    Torres, V.J.2    Skaar, E.P.3
  • 37
    • 0035156408 scopus 로고    scopus 로고
    • Antimicrobial properties of porphyrins
    • DOI 10.1517/13543784.10.2.309
    • I Stojilikovic BD Evavold V Kumar 2001 Antimicrobial properties of porphyrins Expert Opin Investig Drugs 10 309 320 10.1517/13543784.10.2.309 10.1517/13543784.10.2.309 (Pubitemid 32117939)
    • (2001) Expert Opinion on Investigational Drugs , vol.10 , Issue.2 , pp. 309-320
    • Stojiljkovic, I.1    Evavold, B.D.2    Kumar, V.3
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 10.1093/nar/22.22.4673 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • JD Thompson DG Higgins TJ Gibson 1994 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 4673 4680 10.1093/nar/22.22.4673 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide by nano-electrospray mass spectromtry
    • DOI 10.1038/379466a0
    • M Wilm A Shevchenko T Houthaeve S Breit L Schweigerer T Fotsis M Mann 1996 Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry Nature 379 466 469 10.1038/379466a0 8559255 10.1038/379466a0 1:CAS:528:DyaK28XovVagug%3D%3D (Pubitemid 26039530)
    • (1996) Nature , vol.379 , Issue.6564 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 41
    • 0034730333 scopus 로고    scopus 로고
    • A signal transduction system that responds to extracellular iron
    • 10.1016/S0092-8674(00)00092-1 11051552 10.1016/S0092-8674(00)00092-1
    • MMSM Wösten LFF Kox S Chamnongpol FC Soncini EA Groisman 2000 A signal transduction system that responds to extracellular iron Cell 103 113 125 10.1016/S0092-8674(00)00092-1 11051552 10.1016/S0092-8674(00)00092-1
    • (2000) Cell , vol.103 , pp. 113-125
    • Wösten, M.1    Kox, L.F.F.2    Chamnongpol, S.3    Soncini, F.C.4    Groisman, E.A.5
  • 42
    • 17644408373 scopus 로고    scopus 로고
    • Expression of the melC operon in several Streptomyces strains is positively regulated by AdpA, an AraC family transcriptional regulator involved in morphological development in Streptomyces coelicolor
    • DOI 10.1128/JB.187.9.3180-3187.2005
    • D Zhu X He X Zhou Z Deng 2005 Expression of the melC operon in several Streptomyces strains is positively regulated by AdpA, an AraC family transcriptional regulator involved in morphological development in Streptomyces coelicolor J Bacteriol 187 3180 3187 10.1128/JB.187.9.3180-3187.2005 15838045 10.1128/JB.187.9.3180-3187.2005 1:CAS:528:DC%2BD2MXjvVGqtb8%3D (Pubitemid 40571611)
    • (2005) Journal of Bacteriology , vol.187 , Issue.9 , pp. 3180-3187
    • Zhu, D.1    He, X.2    Zhou, X.3    Deng, Z.4
  • 44
    • 0034033246 scopus 로고    scopus 로고
    • The heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase- peroxidase CpeB
    • DOI 10.1046/j.1432-1327.2000.01259.x
    • P Zou H Schrempf 2000 The heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase-peroxidase CpeB Eur J Biochem 267 2840 2849 10.1046/j.1432-1327.2000.01259.x 10806381 10.1046/j.1432-1327.2000.01259.x 1:CAS:528:DC%2BD3cXjs1Gjsro%3D (Pubitemid 30321329)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.10 , pp. 2840-2849
    • Zou, P.1    Schrempf, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.