메뉴 건너뛰기




Volumn 189, Issue 18, 2007, Pages 6521-6531

Regulation of gbpC expression in Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL SURFACE PROTEIN; DEOXYRIBONUCLEASE I; GLUCAN BINDING PROTEIN; PROTEIN COVR; PROTEIN GBPC; UNCLASSIFIED DRUG;

EID: 34548565848     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00825-07     Document Type: Article
Times cited : (59)

References (44)
  • 2
    • 0038010630 scopus 로고    scopus 로고
    • Glucan-binding proteins of the oral streptococci
    • Banas, J. A., and M. M. Vickerman. 2003. Glucan-binding proteins of the oral streptococci. Crit. Rev. Oral Biol. Med. 14:89-99.
    • (2003) Crit. Rev. Oral Biol. Med , vol.14 , pp. 89-99
    • Banas, J.A.1    Vickerman, M.M.2
  • 3
    • 0038643292 scopus 로고    scopus 로고
    • Identification of rocA, a positive regulator of covR expression in the group A streptococcus
    • Biswas, I., and J. R. Scott. 2003. Identification of rocA, a positive regulator of covR expression in the group A streptococcus. J. Bacteriol. 185:3081-3090.
    • (2003) J. Bacteriol , vol.185 , pp. 3081-3090
    • Biswas, I.1    Scott, J.R.2
  • 4
    • 31344435058 scopus 로고    scopus 로고
    • Regulation of the glucosyltransferase (gtfBC) operon by CovR in Streptococcus mutans
    • Biswas, S., and I. Biswas. 2006. Regulation of the glucosyltransferase (gtfBC) operon by CovR in Streptococcus mutans. J. Bacteriol. 188:988-998.
    • (2006) J. Bacteriol , vol.188 , pp. 988-998
    • Biswas, S.1    Biswas, I.2
  • 5
    • 7044235825 scopus 로고    scopus 로고
    • RegM is required for optimal fructosyltransferase and glucosyltransferase gene expression in Streptococcus mutans
    • Browngardt, C. M., Z. T. Wen, and R. A. Burne. 2004. RegM is required for optimal fructosyltransferase and glucosyltransferase gene expression in Streptococcus mutans. FEMS Microbiol. Lett. 240:75-79.
    • (2004) FEMS Microbiol. Lett , vol.240 , pp. 75-79
    • Browngardt, C.M.1    Wen, Z.T.2    Burne, R.A.3
  • 6
    • 0032902762 scopus 로고    scopus 로고
    • Regulation of expression of the fructan hydrolase gene of Streptococcus mutans GS-5 by induction and carbon catabolite repression
    • Burne, R. A., Z. T. Wen, Y. Y. Chen, and J. E. Penders. 1999. Regulation of expression of the fructan hydrolase gene of Streptococcus mutans GS-5 by induction and carbon catabolite repression. J. Bacteriol. 181:2863-2871.
    • (1999) J. Bacteriol , vol.181 , pp. 2863-2871
    • Burne, R.A.1    Wen, Z.T.2    Chen, Y.Y.3    Penders, J.E.4
  • 7
    • 0034909325 scopus 로고    scopus 로고
    • Evolution of a molecular switch: Universal bacterial GTPases regulate ribosome function
    • Caldon, C. E., P. Yoong, and P. E. March. 2001. Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function. Mol. Microbiol. 41:289-297.
    • (2001) Mol. Microbiol , vol.41 , pp. 289-297
    • Caldon, C.E.1    Yoong, P.2    March, P.E.3
  • 9
    • 2942511333 scopus 로고    scopus 로고
    • CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes
    • Dalton, T. L., and J. R. Scott. 2004. CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes. J. Bacteriol. 186:3928-3937.
    • (2004) J. Bacteriol , vol.186 , pp. 3928-3937
    • Dalton, T.L.1    Scott, J.R.2
  • 10
    • 0002379560 scopus 로고    scopus 로고
    • Saliva and the control of plaque pH
    • W. M. Edgar and D. M. O'Mullane ed, 2nd ed. British Dental Association, London, United Kingdom
    • Edgar, W. M., and S. M. Higham. 1996. Saliva and the control of plaque pH, p. 81-94. In W. M. Edgar and D. M. O'Mullane (ed.), Saliva and oral health, 2nd ed. British Dental Association, London, United Kingdom.
    • (1996) Saliva and oral health , pp. 81-94
    • Edgar, W.M.1    Higham, S.M.2
  • 11
    • 0036229494 scopus 로고    scopus 로고
    • Identification of binding sites for the group A streptococcal global regulator CovR
    • Federle, M. J., and J. R. Scott. 2002. Identification of binding sites for the group A streptococcal global regulator CovR. Mol. Microbiol. 43:1161-1172.
    • (2002) Mol. Microbiol , vol.43 , pp. 1161-1172
    • Federle, M.J.1    Scott, J.R.2
  • 12
    • 14644411707 scopus 로고    scopus 로고
    • Environmental pH sensing: Resolving the VirA/VirG two-component system inputs for Agrobacterium pathogenesis
    • Gao, R., and D. G. Lynn. 2005. Environmental pH sensing: resolving the VirA/VirG two-component system inputs for Agrobacterium pathogenesis. J. Bacteriol. 187:2182-2189.
    • (2005) J. Bacteriol , vol.187 , pp. 2182-2189
    • Gao, R.1    Lynn, D.G.2
  • 14
    • 33846936743 scopus 로고    scopus 로고
    • CovR activation of the dipeptide permease promoter (PdppA) in group A streptococcus
    • Gusa, A. A., B. J. Froehlich, D. Desai, V. Stringer, and J. R. Scott. 2007. CovR activation of the dipeptide permease promoter (PdppA) in group A streptococcus. J. Bacteriol. 189:1407-1416.
    • (2007) J. Bacteriol , vol.189 , pp. 1407-1416
    • Gusa, A.A.1    Froehlich, B.J.2    Desai, D.3    Stringer, V.4    Scott, J.R.5
  • 15
    • 33745471491 scopus 로고    scopus 로고
    • Phosphorylation of the group A streptococcal CovR response regulator causes dimerization and promoter-specific recruitment by RNA polymerase
    • Gusa, A. A., J. Gao, V. Stringer, G. Churchward, and J. R. Scott. 2006. Phosphorylation of the group A streptococcal CovR response regulator causes dimerization and promoter-specific recruitment by RNA polymerase. J. Bacteriol. 188:4620-4626.
    • (2006) J. Bacteriol , vol.188 , pp. 4620-4626
    • Gusa, A.A.1    Gao, J.2    Stringer, V.3    Churchward, G.4    Scott, J.R.5
  • 16
    • 19944420855 scopus 로고    scopus 로고
    • The CovR response regulator of group A streptococcus (GAS) acts directly to repress its own promoter
    • Gusa, A. A., and J. R. Scott. 2005. The CovR response regulator of group A streptococcus (GAS) acts directly to repress its own promoter. Mol. Microbiol. 56:1195-1207.
    • (2005) Mol. Microbiol , vol.56 , pp. 1195-1207
    • Gusa, A.A.1    Scott, J.R.2
  • 17
    • 18544408269 scopus 로고    scopus 로고
    • The PmrA-PmrB two-component system responding to acidic pH and iron controls virulence in the plant pathogen Erwinia carotovora ssp. carotovora
    • Hyytiainen, H., S. Sjoblom, T. Palomaki, A. Tuikkala, and E. Tapio Palva. 2003. The PmrA-PmrB two-component system responding to acidic pH and iron controls virulence in the plant pathogen Erwinia carotovora ssp. carotovora. Mol. Microbiol. 50:795-807.
    • (2003) Mol. Microbiol , vol.50 , pp. 795-807
    • Hyytiainen, H.1    Sjoblom, S.2    Palomaki, T.3    Tuikkala, A.4    Tapio Palva, E.5
  • 19
    • 0028337422 scopus 로고
    • Genetic analysis of fructan-hyper-producing strains of Streptococcus mutans
    • Kiska, D. L., and F. L. Macrina. 1994. Genetic analysis of fructan-hyper-producing strains of Streptococcus mutans. Infect. Immun. 62:2679-2686.
    • (1994) Infect. Immun , vol.62 , pp. 2679-2686
    • Kiska, D.L.1    Macrina, F.L.2
  • 20
    • 0027530878 scopus 로고
    • Virulence factors of mutans streptococci: Role of molecular genetics
    • Kuramitsu, H. 1993. Virulence factors of mutans streptococci: role of molecular genetics. Crit. Rev. Oral. Biol. Med. 4:159-176.
    • (1993) Crit. Rev. Oral. Biol. Med , vol.4 , pp. 159-176
    • Kuramitsu, H.1
  • 21
    • 0034779082 scopus 로고    scopus 로고
    • Regulation of the gtfBC and ftf genes of Streptococcus mutans in biofilms in response to pH and carbohydrate
    • Li, Y., and R. A. Burne. 2001. Regulation of the gtfBC and ftf genes of Streptococcus mutans in biofilms in response to pH and carbohydrate. Microbiology 147:2841-2848.
    • (2001) Microbiology , vol.147 , pp. 2841-2848
    • Li, Y.1    Burne, R.A.2
  • 22
    • 0036844205 scopus 로고    scopus 로고
    • Novel two-component regulatory system involved in biofilm formation and acid resistance in Streptococcus mutans
    • Li, Y. H., P. C. Lau, N. Tang, G. Svensater, R. P. Ellen, and D. G. Cvitkovitch. 2002. Novel two-component regulatory system involved in biofilm formation and acid resistance in Streptococcus mutans. J. Bacteriol. 184:6333-6342.
    • (2002) J. Bacteriol , vol.184 , pp. 6333-6342
    • Li, Y.H.1    Lau, P.C.2    Tang, N.3    Svensater, G.4    Ellen, R.P.5    Cvitkovitch, D.G.6
  • 23
    • 0033965303 scopus 로고    scopus 로고
    • Streptococcus gordonii biofilm formation: Identification of genes that code for biofilm phenotypes
    • Loo, C. Y., D. A. Corliss, and N. Ganeshkumar. 2000. Streptococcus gordonii biofilm formation: identification of genes that code for biofilm phenotypes. J. Bacteriol. 182:1374-1382.
    • (2000) J. Bacteriol , vol.182 , pp. 1374-1382
    • Loo, C.Y.1    Corliss, D.A.2    Ganeshkumar, N.3
  • 24
    • 33846973663 scopus 로고    scopus 로고
    • Glucan-binding proteins are essential for shaping Streptococcus mutans biofilm architecture
    • Lynch, D. J., T. L. Fountain, J. E. Mazurkiewicz, and J. A. Banas. 2007. Glucan-binding proteins are essential for shaping Streptococcus mutans biofilm architecture. FEMS Microbiol. Lett. 268:158-165.
    • (2007) FEMS Microbiol. Lett , vol.268 , pp. 158-165
    • Lynch, D.J.1    Fountain, T.L.2    Mazurkiewicz, J.E.3    Banas, J.A.4
  • 27
    • 33645068631 scopus 로고    scopus 로고
    • Binding of glucan-binding protein C to GTFD-synthesized soluble glucan in sucrose-dependent adhesion of Streptococcus mutans
    • Matsumoto, M., K. Fujita, and T. Ooshima. 2006. Binding of glucan-binding protein C to GTFD-synthesized soluble glucan in sucrose-dependent adhesion of Streptococcus mutans. Oral Microbiol. Immunol. 21:42-46.
    • (2006) Oral Microbiol. Immunol , vol.21 , pp. 42-46
    • Matsumoto, M.1    Fujita, K.2    Ooshima, T.3
  • 29
    • 33744744718 scopus 로고    scopus 로고
    • Functional analysis of glucan binding protein B from Streptococcus mutans
    • Mattos-Graner, R. O., K. A. Porter, D. J. Smith, Y. Hosogi, and M. J. Duncan. 2006. Functional analysis of glucan binding protein B from Streptococcus mutans. J. Bacteriol. 188:3813-3825.
    • (2006) J. Bacteriol , vol.188 , pp. 3813-3825
    • Mattos-Graner, R.O.1    Porter, K.A.2    Smith, D.J.3    Hosogi, Y.4    Duncan, M.J.5
  • 30
    • 0022650957 scopus 로고
    • The effect of lowering the pH on the composition and metabolism of a community of nine oral bacteria grown in a chemostat
    • McDermid, A. S., A. S. McKee, D. C. Ellwood, and P. D. Marsh. 1986. The effect of lowering the pH on the composition and metabolism of a community of nine oral bacteria grown in a chemostat. J. Gen. Microbiol. 132:1205-1214.
    • (1986) J. Gen. Microbiol , vol.132 , pp. 1205-1214
    • McDermid, A.S.1    McKee, A.S.2    Ellwood, D.C.3    Marsh, P.D.4
  • 31
    • 23744455757 scopus 로고    scopus 로고
    • LuxS controls bacteriocin production in Streptococcus mutans through a novel regulatory component
    • Merritt, J., J. Kreth, W. Shi, and F. Qi. 2005. LuxS controls bacteriocin production in Streptococcus mutans through a novel regulatory component. Mol. Microbiol. 57:960-969.
    • (2005) Mol. Microbiol , vol.57 , pp. 960-969
    • Merritt, J.1    Kreth, J.2    Shi, W.3    Qi, F.4
  • 33
    • 0035983372 scopus 로고    scopus 로고
    • Attenuation of glucan-binding protein C reduces the cariogenicity of Streptococcus mutans: Analysis of strains isolated from human blood
    • Nakano, K., M. Matsumura, M. Kawaguchi, T. Fujiwara, S. Sobue, I. Nakagawa, S. Hamada, and T. Ooshima. 2002. Attenuation of glucan-binding protein C reduces the cariogenicity of Streptococcus mutans: analysis of strains isolated from human blood. J. Dent. Res. 81:376-379.
    • (2002) J. Dent. Res , vol.81 , pp. 376-379
    • Nakano, K.1    Matsumura, M.2    Kawaguchi, M.3    Fujiwara, T.4    Sobue, S.5    Nakagawa, I.6    Hamada, S.7    Ooshima, T.8
  • 34
    • 4143076907 scopus 로고    scopus 로고
    • Contribution of glucan-binding protein C of Streptococcus mutans to bacteremia occurrence
    • Nomura, R., K. Nakano, and T. Ooshima. 2004. Contribution of glucan-binding protein C of Streptococcus mutans to bacteremia occurrence. Arch. Oral Biol. 49:783-788.
    • (2004) Arch. Oral Biol , vol.49 , pp. 783-788
    • Nomura, R.1    Nakano, K.2    Ooshima, T.3
  • 36
    • 0037767739 scopus 로고    scopus 로고
    • X in Streptococcus pyogenes is restricted at two levels. J. Bacteriol. 185:4291-4297.
    • X in Streptococcus pyogenes is restricted at two levels. J. Bacteriol. 185:4291-4297.
  • 37
    • 33750799914 scopus 로고    scopus 로고
    • The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin, Y., N. Polacek, O. Vesper, E. Staub, E. Einfeldt, D. N. Wilson, and K. H. Nierhaus. 2006. The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127:721-733.
    • (2006) Cell , vol.127 , pp. 721-733
    • Qin, Y.1    Polacek, N.2    Vesper, O.3    Staub, E.4    Einfeldt, E.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 38
    • 33846912421 scopus 로고    scopus 로고
    • Unraveling the regulatory network in Streptococcus pyogenes: The global response regulator CovR represses rivR directly
    • Roberts, S. A., G. G. Churchward, and J. R. Scott. 2007. Unraveling the regulatory network in Streptococcus pyogenes: the global response regulator CovR represses rivR directly. J. Bacteriol. 189:1459-1463.
    • (2007) J. Bacteriol , vol.189 , pp. 1459-1463
    • Roberts, S.A.1    Churchward, G.G.2    Scott, J.R.3
  • 39
    • 0036443740 scopus 로고    scopus 로고
    • The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis
    • Ryan, K. R., E. M. Judd, and L. Shapiro. 2002. The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis. J. Mol. Biol. 324:443-455.
    • (2002) J. Mol. Biol , vol.324 , pp. 443-455
    • Ryan, K.R.1    Judd, E.M.2    Shapiro, L.3
  • 40
    • 0031036878 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans
    • Sato, Y., Y. Yamamoto, and H. Kizaki. 1997. Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans. Infect. Immun. 65:668-675.
    • (1997) Infect. Immun , vol.65 , pp. 668-675
    • Sato, Y.1    Yamamoto, Y.2    Kizaki, H.3
  • 41
    • 0034607978 scopus 로고    scopus 로고
    • Construction of region-specific partial duplication mutants (merodiploid mutants) to identify the regulatory gene for the glucan-binding protein C gene in vivo in Streptococcus mutans
    • Sato, Y., Y. Yamamoto, and H. Kizaki. 2000. Construction of region-specific partial duplication mutants (merodiploid mutants) to identify the regulatory gene for the glucan-binding protein C gene in vivo in Streptococcus mutans. FEMS Microbiol. Lett. 186:187-191.
    • (2000) FEMS Microbiol. Lett , vol.186 , pp. 187-191
    • Sato, Y.1    Yamamoto, Y.2    Kizaki, H.3
  • 42
    • 0034572447 scopus 로고    scopus 로고
    • Xylitol-induced elevated expression of the gbpC gene in a population of Streptococcus mutans cells
    • Sato, Y., Y. Yamamoto, and H. Kizaki. 2000. Xylitol-induced elevated expression of the gbpC gene in a population of Streptococcus mutans cells. Eur. J. Oral Sci. 108:538-545.
    • (2000) Eur. J. Oral Sci , vol.108 , pp. 538-545
    • Sato, Y.1    Yamamoto, Y.2    Kizaki, H.3
  • 44
    • 0027512967 scopus 로고
    • Streptococcus mutans fructosyltransferase (ftf) and glucosyltransferase (gtfBC) operon fusion strains in continuous culture
    • Wexler, D. L., M. C. Hudson, and R. A. Burne. 1993. Streptococcus mutans fructosyltransferase (ftf) and glucosyltransferase (gtfBC) operon fusion strains in continuous culture. Infect. Immun. 61:1259-1267.
    • (1993) Infect. Immun , vol.61 , pp. 1259-1267
    • Wexler, D.L.1    Hudson, M.C.2    Burne, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.