메뉴 건너뛰기




Volumn 7, Issue 2, 2012, Pages

A novel two-component system involved in the transition to secondary metabolism in Streptomyces coelicolor

Author keywords

[No Author keywords available]

Indexed keywords

ACTINORHODINE; PROTEIN HISTIDINE KINASE; REGULATOR PROTEIN; ANTIINFECTIVE AGENT;

EID: 84856805770     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0031760     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0033925731 scopus 로고    scopus 로고
    • Primary metabolism and its control in streptomycetes: a most unusual group of bacteria
    • Hodgson DA, (2000) Primary metabolism and its control in streptomycetes: a most unusual group of bacteria. Adv Microb Physiol 42: 41-238.
    • (2000) Adv Microb Physiol , vol.42 , pp. 41-238
    • Hodgson, D.A.1
  • 2
    • 0031747318 scopus 로고    scopus 로고
    • Taking a genetic scalpel to the Streptomyces colony
    • Chater KF, (1998) Taking a genetic scalpel to the Streptomyces colony. Microbiology 144: 1465-1478.
    • (1998) Microbiology , vol.144 , pp. 1465-1478
    • Chater, K.F.1
  • 5
    • 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)
    • Hutchings MI, Hoskisson PA, Chandra G, Buttner MJ, (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.
    • (2004) Microbiology , vol.150 , pp. 2795-2806
    • Hutchings, M.I.1    Hoskisson, P.A.2    Chandra, G.3    Buttner, M.J.4
  • 6
    • 0035883922 scopus 로고    scopus 로고
    • DNA microarray analysis of Bacillus subtilis DegU, ComA and PhoP regulons: an approach to comprehensive analysis of B. subtilis two-component regulatory systems
    • Ogura M, Yamaguchi H, Yoshida K, Fujita Y, Tanaka T, (2001) DNA microarray analysis of Bacillus subtilis DegU, ComA and PhoP regulons: an approach to comprehensive analysis of B. subtilis two-component regulatory systems. Nucl Acids Res 29: 3804-3813.
    • (2001) Nucl Acids Res , vol.29 , pp. 3804-3813
    • Ogura, M.1    Yamaguchi, H.2    Yoshida, K.3    Fujita, Y.4    Tanaka, T.5
  • 7
    • 0036456146 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: genome-widw analysis of the DegS-DegU regulon by transcriptomics and proteomics
    • Mäder U, Antelmann H, Buder T, Dahl MK, Hecker M, et al. (2002) Bacillus subtilis functional genomics: genome-widw analysis of the DegS-DegU regulon by transcriptomics and proteomics. Mol Genet Genomics 268: 455-467.
    • (2002) Mol Genet Genomics , vol.268 , pp. 455-467
    • Mäder, U.1    Antelmann, H.2    Buder, T.3    Dahl, M.K.4    Hecker, M.5
  • 8
    • 78650385274 scopus 로고    scopus 로고
    • Repression of antibiotic production and sporulation in Streptomyces coelicolor by overexpression of a TetR family transcriptional regulator
    • Xu D, Seghezzi N, Esnaultand C, Virolle MJ, (2010) Repression of antibiotic production and sporulation in Streptomyces coelicolor by overexpression of a TetR family transcriptional regulator. Appl Environ Microbiol 73: 7741-7753.
    • (2010) Appl Environ Microbiol , vol.73 , pp. 7741-7753
    • Xu, D.1    Seghezzi, N.2    Esnaultand, C.3    Virolle, M.J.4
  • 9
    • 18844397802 scopus 로고    scopus 로고
    • Transcriptome analyis of the secretion stress response of Bacillus subtilis
    • Hyyryläinen HL, Sarvas M, Kontinen VP, (2005) Transcriptome analyis of the secretion stress response of Bacillus subtilis. Appl Microbiol Biotecnol 67: 389-396.
    • (2005) Appl Microbiol Biotecnol , vol.67 , pp. 389-396
    • Hyyryläinen, H.L.1    Sarvas, M.2    Kontinen, V.P.3
  • 10
    • 38349086492 scopus 로고    scopus 로고
    • The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2)
    • Hesketh A, Chen JW, Ryding J, Chang S, Bibb M, (2007) The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2). Genome Biol 8: R161.1-R161.18.
    • (2007) Genome Biol , vol.8 , pp. 1-18
    • Hesketh, A.1    Chen, J.W.2    Ryding, J.3    Chang, S.4    Bibb, M.5
  • 11
    • 17544367082 scopus 로고    scopus 로고
    • A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls antibiotic biosynthtic genes
    • Martinez-Costa OH, Arias P, Romero NM, Parro V, Mellado RP, et al. (1996) A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls antibiotic biosynthtic genes. J Biol Chem 271: 10627-10634.
    • (1996) J Biol Chem , vol.271 , pp. 10627-10634
    • Martinez-Costa, O.H.1    Arias, P.2    Romero, N.M.3    Parro, V.4    Mellado, R.P.5
  • 12
    • 0035036356 scopus 로고    scopus 로고
    • Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2)
    • Sun J, Hesketh A, Bibb MJ, (2001) Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2). J Bacteriol 183: 3488-3498.
    • (2001) J Bacteriol , vol.183 , pp. 3488-3498
    • Sun, J.1    Hesketh, A.2    Bibb, M.J.3
  • 13
    • 38949102057 scopus 로고    scopus 로고
    • Manipulating and understanding antibiotic production in Streptomyces coelicolor A3(2) with decoy oligonucleotides
    • McArthur M, Bibb MJ, (2008) Manipulating and understanding antibiotic production in Streptomyces coelicolor A3(2) with decoy oligonucleotides. Proc Nat Acad Sci USA 105: 1010-1025.
    • (2008) Proc Nat Acad Sci USA , vol.105 , pp. 1010-1025
    • McArthur, M.1    Bibb, M.J.2
  • 14
    • 33750117809 scopus 로고    scopus 로고
    • Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis
    • Escutia MR, Val G, Palacín A, Geukens N, Anné J, et al. (2006) Compensatory effect of the minor Streptomyces lividans type I signal peptidases on the SipY major signal peptidase deficiency as determined by extracellular proteome analysis. Proteomics 6: 4137-4146.
    • (2006) Proteomics , vol.6 , pp. 4137-4146
    • Escutia, M.R.1    Val, G.2    Palacín, A.3    Geukens, N.4    Anné, J.5
  • 15
    • 71649085969 scopus 로고    scopus 로고
    • Evaluation of isotope-coded protein labeling (ICPL) in the quantitative analysis of complex proteomes
    • Paradela A, Marcilla M, Navajas R, Ferreira L, Ramos-Fernandez A, et al. (2010) Evaluation of isotope-coded protein labeling (ICPL) in the quantitative analysis of complex proteomes. Talanta 80: 1496-502.
    • (2010) Talanta , vol.80 , pp. 1496-1502
    • Paradela, A.1    Marcilla, M.2    Navajas, R.3    Ferreira, L.4    Ramos-Fernandez, A.5
  • 16
    • 77953846853 scopus 로고    scopus 로고
    • Differential proteomic analysis using isotope-coded protein labeling strategies: comparison, improvements and application to simulated microgravity effect on Cupriavidus metallidurans CH34
    • Leroy B, Rosier C, Erculisse V, Leys N, Mergeay M, et al. (2010) Differential proteomic analysis using isotope-coded protein labeling strategies: comparison, improvements and application to simulated microgravity effect on Cupriavidus metallidurans CH34. Proteomics 10: 2281-2291.
    • (2010) Proteomics , vol.10 , pp. 2281-2291
    • Leroy, B.1    Rosier, C.2    Erculisse, V.3    Leys, N.4    Mergeay, M.5
  • 17
    • 38649084424 scopus 로고    scopus 로고
    • Secreted-Protein response to sigma U activity in Streptomyces coelicolor
    • Gordon ND, Ottaviano GL, Connell SE, Tobkin GV, Son CH, et al. (2008) Secreted-Protein response to sigma U activity in Streptomyces coelicolor. J Bacteriol 190: 894-904.
    • (2008) J Bacteriol , vol.190 , pp. 894-904
    • Gordon, N.D.1    Ottaviano, G.L.2    Connell, S.E.3    Tobkin, G.V.4    Son, C.H.5
  • 18
    • 33845199230 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor
    • Widdick D, Dilks A, Chandra K, Bottrill G, Naldrett A, et al. (2006) The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor. Proc Nat Acad Sci USA 103: 17927-17932.
    • (2006) Proc Nat Acad Sci USA , vol.103 , pp. 17927-17932
    • Widdick, D.1    Dilks, A.2    Chandra, K.3    Bottrill, G.4    Naldrett, A.5
  • 19
    • 0036223585 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis
    • Eymann C, Homuth G, Scharf C, Hecker M, (2002) Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis. J Bacteriol 184: 2500-2520.
    • (2002) J Bacteriol , vol.184 , pp. 2500-2520
    • Eymann, C.1    Homuth, G.2    Scharf, C.3    Hecker, M.4
  • 20
    • 0003728297 scopus 로고
    • Genetic manipulation of Streptomyces
    • A laboratory manual. John Innes Foundation, Norwich, UK
    • Hopwood DA, Bibb MJ, Chater KF, (1985) Genetic manipulation of Streptomyces. A laboratory manual. John Innes Foundation, Norwich, UK.
    • (1985)
    • Hopwood, D.A.1    Bibb, M.J.2    Chater, K.F.3
  • 22
    • 0036718560 scopus 로고    scopus 로고
    • SipY is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion
    • Palacín A, Parro V, Geukens N, Anné J, Mellado RP, (2002) SipY is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion. J Bacteriol 184: 4875-4880.
    • (2002) J Bacteriol , vol.184 , pp. 4875-4880
    • Palacín, A.1    Parro, V.2    Geukens, N.3    Anné, J.4    Mellado, R.P.5
  • 23
    • 0033047685 scopus 로고    scopus 로고
    • A putative two component signal transduction system regulates sigma E, a sigma factor required for normal cell wall integrity in Streptomyces coelicolor A3(2)
    • Paget MSB, Leibovitz E, Buttner MJ, (1999) A putative two component signal transduction system regulates sigma E, a sigma factor required for normal cell wall integrity in Streptomyces coelicolor A3(2). Mol Microbiol 33: 97-107.
    • (1999) Mol Microbiol , vol.33 , pp. 97-107
    • Paget, M.S.B.1    Leibovitz, E.2    Buttner, M.J.3
  • 24
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical Bayes methods for assessing differential expression in microarray experiments
    • Article 3 URL
    • Smyth GK, (2004) Linear models and empirical Bayes methods for assessing differential expression in microarray experiments. Stat Appl Genet Mol Biol 3 Article 3 URLhttp://www.bepress.com/sagm/vol3/iss1/art3.
    • (2004) Stat Appl Genet Mol Biol , vol.3
    • Smyth, G.K.1
  • 25
    • 0242333835 scopus 로고    scopus 로고
    • Normalization of cDNA microarray data
    • Smyth GK, Speed T, (2003) Normalization of cDNA microarray data. Methods 31: 265-273.
    • (2003) Methods , vol.31 , pp. 265-273
    • Smyth, G.K.1    Speed, T.2
  • 26
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y, (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Roy Stat Soc 57: 289-300.
    • (1995) J Roy Stat Soc , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 27
    • 0942268841 scopus 로고    scopus 로고
    • Functional angucycline-like antibiotic gene cluster in the terminal inverted repeats of the Streptomyces ambofaciens linear chromosome
    • Pang X, Aigle B, Girardet JM, Mangenot S, Pernodet JL, et al. (2004) Functional angucycline-like antibiotic gene cluster in the terminal inverted repeats of the Streptomyces ambofaciens linear chromosome. Antimicro Agents Chemother 48: 575-588.
    • (2004) Antimicro Agents Chemother , vol.48 , pp. 575-588
    • Pang, X.1    Aigle, B.2    Girardet, J.M.3    Mangenot, S.4    Pernodet, J.L.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (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
  • 29
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg 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
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4    Scheibe, B.5
  • 30
    • 0031807109 scopus 로고    scopus 로고
    • Use if thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud T, (1998) Use if thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19: 758-760.
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 31
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M, (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 32
    • 10044248655 scopus 로고    scopus 로고
    • Statistical model for large-scale peptide identification in databases from tandem mass spectra using SEQUEST
    • López-Ferrer D, Martínez-Bartolomé S, Villar M, Campillos M, Martín-Maroto F, et al. (2004) Statistical model for large-scale peptide identification in databases from tandem mass spectra using SEQUEST. Anal Chem 76: 6853-6860.
    • (2004) Anal Chem , vol.76 , pp. 6853-6860
    • López-Ferrer, D.1    Martínez-Bartolomé, S.2    Villar, M.3    Campillos, M.4    Martín-Maroto, F.5
  • 33
    • 0025025408 scopus 로고
    • Effect of inhibitory activity of mutation at reaction site P4 of the Streptomyces subtilisin inhibitor, SSI
    • Kojima S, Kumagai I, Miura K, (1990) Effect of inhibitory activity of mutation at reaction site P4 of the Streptomyces subtilisin inhibitor, SSI. Protein Eng 3: 527-530.
    • (1990) Protein Eng , vol.3 , pp. 527-530
    • Kojima, S.1    Kumagai, I.2    Miura, K.3
  • 36
    • 0032213555 scopus 로고    scopus 로고
    • The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tü22: sequence analysis and expression in a heterologous host
    • lchinose K, Bedford DJ, Tornus D, Bechthold A, Bibb MJ, et al. (1998) The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tü22: sequence analysis and expression in a heterologous host. Chem Biol 5: 647-659.
    • (1998) Chem Biol , vol.5 , pp. 647-659
    • Lchinose, K.1    Bedford, D.J.2    Tornus, D.3    Bechthold, A.4    Bibb, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.