메뉴 건너뛰기




Volumn 259, Issue 2, 1998, Pages 224-232

Identification of the DNA-binding sites for two response regulators involved in control of bacteriocin synthesis in Lactobacillus plantarum C11

Author keywords

Bacteriocin synthesis; DNA binding; Regulation; Response regulator

Indexed keywords

BACTERIOCIN; DNA BINDING PROTEIN; HISTIDINE; PHEROMONE; PHOSPHOTRANSFERASE;

EID: 0031662663     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050808     Document Type: Article
Times cited : (46)

References (35)
  • 1
    • 0028282042 scopus 로고
    • Protein histidine kinases and signal transduction in prokaryotes and eukaryotes
    • Alex LA, Simon MI (1994) Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet 10:133-138
    • (1994) Trends Genet , vol.10 , pp. 133-138
    • Alex, L.A.1    Simon, M.I.2
  • 2
    • 0025908814 scopus 로고
    • Signal transduction pathways involving protein phosphorylation in prokaryotes
    • Bourret RB, Borkovich KA, Simon MI (1991) Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu Rev Biochem 60:401-441
    • (1991) Annu Rev Biochem , vol.60 , pp. 401-441
    • Bourret, R.B.1    Borkovich, K.A.2    Simon, M.I.3
  • 3
    • 0030779483 scopus 로고    scopus 로고
    • Pheromone-induced production of antimicrobial peptides in Lactobacillus
    • Brurberg MB, Nes IF, Eijsink VGH (1997) Pheromone-induced production of antimicrobial peptides in Lactobacillus. Mol Microbiol 26:347-360
    • (1997) Mol Microbiol , vol.26 , pp. 347-360
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 4
    • 0028052910 scopus 로고
    • The gene encoding Plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system
    • Diep DB, Håvarstein LS, Nissen-Meyer J, Nes IF (1994) The gene encoding Plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system. Appl Environ microbiol 60:160-166
    • (1994) Appl Environ Microbiol , vol.60 , pp. 160-166
    • Diep, D.B.1    Håvarstein, L.S.2    Nissen-Meyer, J.3    Nes, I.F.4
  • 5
    • 0029565798 scopus 로고
    • A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11
    • Diep DB, Håvarstein LS, Nes IF (1995) A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol Microbiol 18:631-639
    • (1995) Mol Microbiol , vol.18 , pp. 631-639
    • Diep, D.B.1    Håvarstein, L.S.2    Nes, I.F.3
  • 6
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • Diep DB, Håvarstein LS, Nes IF (1996) Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J Bacteriol 178:4472-483
    • (1996) J Bacteriol , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Håvarstein, L.S.2    Nes, I.F.3
  • 7
    • 0029989630 scopus 로고    scopus 로고
    • Induction of bacteriocin production in Lactobacillus sake by a secreted peptide
    • Eijsink VGH, Brurberg MB, Middelhoven PH, Nes IF (1996) Induction of bacteriocin production in Lactobacillus sake by a secreted peptide. J Bacteriol 178:2232-2237
    • (1996) J Bacteriol , vol.178 , pp. 2232-2237
    • Eijsink, V.G.H.1    Brurberg, M.B.2    Middelhoven, P.H.3    Nes, I.F.4
  • 8
    • 0026662751 scopus 로고
    • Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli
    • Feng J, Atkinson MR, McClearly W, Stock JB, Wanner BL, Ninfa AJ (1992) Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli. J Bacteriol 174:6061-6070
    • (1992) J Bacteriol , vol.174 , pp. 6061-6070
    • Feng, J.1    Atkinson, M.R.2    McClearly, W.3    Stock, J.B.4    Wanner, B.L.5    Ninfa, A.J.6
  • 9
    • 0024323026 scopus 로고
    • Measurement of protein-DNA interaction parameters by electrophoresis mobility shift assay
    • Fried MG (1989) Measurement of protein-DNA interaction parameters by electrophoresis mobility shift assay. Electrophoresis 10:366-376
    • (1989) Electrophoresis , vol.10 , pp. 366-376
    • Fried, M.G.1
  • 10
    • 10344221578 scopus 로고    scopus 로고
    • The DnrN protein of Streptomyces peucetius, a pseudo-response regulator, is a DNA-binding protein involved in the regulation of daunorubicin biosynthesis
    • Furuya K, Hutchinson R (1996) The DnrN protein of Streptomyces peucetius, a pseudo-response regulator, is a DNA-binding protein involved in the regulation of daunorubicin biosynthesis. J Bacteriol 178:6310-6318
    • (1996) J Bacteriol , vol.178 , pp. 6310-6318
    • Furuya, K.1    Hutchinson, R.2
  • 11
  • 12
    • 0002014616 scopus 로고
    • agr: A polycistronic locus regulating exoprotein synthesis in Staphylococcus aureus
    • Novick RP (ed) VCH Publishers, New York
    • Kornblum J, Kreiswirth B, Projan SJ, Ross H, Novick RP (1990) agr: a polycistronic locus regulating exoprotein synthesis in Staphylococcus aureus. In: Novick RP (ed) Molecular biology of the staphylococci. VCH Publishers, New York, pp 373-402
    • (1990) Molecular Biology of the Staphylococci , pp. 373-402
    • Kornblum, J.1    Kreiswirth, B.2    Projan, S.J.3    Ross, H.4    Novick, R.P.5
  • 13
    • 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
  • 14
    • 0030809030 scopus 로고    scopus 로고
    • Bacillus subtilis PhoP Binds to the phob tandem promoter exclusively within the phosphate starvation-inducible promoter
    • Liu W, Hulett FM (1997) Bacillus subtilis PhoP Binds to the phob tandem promoter exclusively within the phosphate starvation-inducible promoter. J Bacteriol 179:6302-6310
    • (1997) J Bacteriol , vol.179 , pp. 6302-6310
    • Liu, W.1    Hulett, F.M.2
  • 15
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight Phospho-donors
    • Lukat GS, McCleary WR, Stock AM, Stock JB (1992) Phosphorylation of bacterial response regulator proteins by low molecular weight Phospho-donors. Proc Natl Acad Sci USA 89:718-722
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 16
    • 0024347198 scopus 로고
    • Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis
    • Lupas A, Stock JB (1989) Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J Biol Chem 264:17337-17342
    • (1989) J Biol Chem , vol.264 , pp. 17337-17342
    • Lupas, A.1    Stock, J.B.2
  • 17
    • 0029858049 scopus 로고    scopus 로고
    • Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: Characterization of DNA-binding at target promoters
    • Lynch AS, Lin ECC (1996) Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA-binding at target promoters. J Bacteriol 178:6238-6249
    • (1996) J Bacteriol , vol.178 , pp. 6238-6249
    • Lynch, A.S.1    Lin, E.C.C.2
  • 18
    • 0027207516 scopus 로고
    • Is acetyl phosphate a global signal in Escherichia coli?
    • McClearly WR, Stock JB, Ninfa AJ (1983) Is acetyl phosphate a global signal in Escherichia coli? J Bacteriol 175:2793-2798
    • (1983) J Bacteriol , vol.175 , pp. 2793-2798
    • McClearly, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 19
    • 0030271449 scopus 로고    scopus 로고
    • Detection of the response regulator AgrA in the cytosolic fraction of Staphylococcus aureus by monoclonal antibodies
    • Morfeldt E, Panova-Sapundjieva I, Gustafson B, Arvidson S (1996a) Detection of the response regulator AgrA in the cytosolic fraction of Staphylococcus aureus by monoclonal antibodies. FEMS Microbiol Lett 143:195-201
    • (1996) FEMS Microbiol Lett , vol.143 , pp. 195-201
    • Morfeldt, E.1    Panova-Sapundjieva, I.2    Gustafson, B.3    Arvidson, S.4
  • 20
    • 0029814352 scopus 로고    scopus 로고
    • Transcriptional control of the agr-dependent virulence gene regulator, RNAIII, in Staphylococcus aureus
    • Morefeldt E, Tegmark K, Arvidson S (1996b) Transcriptional control of the agr-dependent virulence gene regulator, RNAIII, in Staphylococcus aureus. Mol Microbiol 21:1227-1237
    • (1996) Mol Microbiol , vol.21 , pp. 1227-1237
    • Morefeldt, E.1    Tegmark, K.2    Arvidson, S.3
  • 22
    • 0026069669 scopus 로고
    • Protein phosphorylation and the regulation of cellular processes by the homologous two-component regulatory systems of bacteria
    • Ninfa AJ (1991) Protein phosphorylation and the regulation of cellular processes by the homologous two-component regulatory systems of bacteria. Genet Engin 13:39-72
    • (1991) Genet Engin , vol.13 , pp. 39-72
    • Ninfa, A.J.1
  • 23
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer J, Holo H, Håvarstein LS, Sietten K, Nes IF (1992) A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J Bacteriol 174:5686-5692
    • (1992) J Bacteriol , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Håvarstein, L.S.3    Sietten, K.4    Nes, I.F.5
  • 25
    • 0002113982 scopus 로고
    • Genetic approaches for signaling pathways and proteins
    • Hoch JA, Silhavy TJ (eds) ASM Press, Washington DC
    • Parkinson JS (1995) Genetic approaches for signaling pathways and proteins. In: Hoch JA, Silhavy TJ (eds) Two-component signal transduction. ASM Press, Washington DC, pp 9-23
    • (1995) Two-component Signal Transduction , pp. 9-23
    • Parkinson, J.S.1
  • 26
    • 0029745349 scopus 로고    scopus 로고
    • Regulation of competence for genetic transformation in Streptococcus pneumoniae by an auto-induced peptide pheromone and a two-component regulatory system
    • Pestova EV, Håvarstein LS, Morrison DA (1996) Regulation of competence for genetic transformation in Streptococcus pneumoniae by an auto-induced peptide pheromone and a two-component regulatory system, Mol Microbiol 21:853-862
    • (1996) Mol Microbiol , vol.21 , pp. 853-862
    • Pestova, E.V.1    Håvarstein, L.S.2    Morrison, D.A.3
  • 28
    • 0029014937 scopus 로고
    • Induction of bacteriocin in Carnobacterium piscicola LV17
    • Saucier L, Poon A, Stiles ME (1995) Induction of bacteriocin in Carnobacterium piscicola LV17. J Appl Bacteriol 78:684-690
    • (1995) J Appl Bacteriol , vol.78 , pp. 684-690
    • Saucier, L.1    Poon, A.2    Stiles, M.E.3
  • 29
    • 0025291634 scopus 로고
    • Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coli
    • Stewart RC, Roth AF, Dahlquist FW (1990) Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coli. J Bacteriol 172:3388-3399
    • (1990) J Bacteriol , vol.172 , pp. 3388-3399
    • Stewart, R.C.1    Roth, A.F.2    Dahlquist, F.W.3
  • 30
    • 0018104398 scopus 로고
    • A protein methylesterase involved in bacterial sensing
    • Stock JB, Koshland DE Jr (1978) A protein methylesterase involved in bacterial sensing. Proc Natl Acad Sci USA 75:3659-3663
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3659-3663
    • Stock, J.B.1    Koshland Jr., D.E.2
  • 31
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock JB, Ninia AJ, Stock AM (1989) Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev 53: 450-490
    • (1989) Microbiol Rev , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninia, A.J.2    Stock, A.M.3
  • 32
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis
    • Hoch JA, Silhavy TJ (eds) ASM Press, Washington DC
    • Stock JB, Surette MG, Levit M, Park P (1995) Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis. In: Hoch JA, Silhavy TJ (eds) Two-component signal transduction. ASM Press, Washington DC, pp 25-51
    • (1995) Two-component Signal Transduction , pp. 25-51
    • Stock, J.B.1    Surette, M.G.2    Levit, M.3    Park, P.4
  • 34
    • 0028138668 scopus 로고
    • Histidine and aspartate phosphorylation: Two-component systems and the limits of homology
    • Swanson RV, Alex LA, Simon MI (1994) Histidine and aspartate phosphorylation: two-component systems and the limits of homology. Trends Biochem Sci 19:485-490
    • (1994) Trends Biochem Sci , vol.19 , pp. 485-490
    • Swanson, R.V.1    Alex, L.A.2    Simon, M.I.3
  • 35
    • 0002946893 scopus 로고
    • Structural and functional conservation in response regulators
    • Hoch JA, Silhavy TJ (eds) ASM Press, Washington DC
    • Volz K (1995) Structural and functional conservation in response regulators. In: Hoch JA, Silhavy TJ (eds) Two-component signal transduction. ASM Press, Washington DC, pp 53-64
    • (1995) Two-component Signal Transduction , pp. 53-64
    • Volz, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.