메뉴 건너뛰기




Volumn 75, Issue 5, 2010, Pages 1145-1158

Seryl-phosphorylated HPr regulates CcpA-independent carbon catabolite repression in conjunction with PTS permeases in Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CATABOLITE CONTROL PROTEIN A; CELLOBIOSE; FRUCTAN; HPR PROTEIN; LACTOSE; PERMEASE; PHOSPHOTRANSFERASE; SERINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARBON; CARRIER PROTEIN; PHOSPHOCARRIER PROTEIN HPR; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE;

EID: 77349124258     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.07029.x     Document Type: Article
Times cited : (54)

References (48)
  • 1
    • 0042029402 scopus 로고    scopus 로고
    • Characterization of Streptococcus mutans strains deficient in EIIAB Man of the sugar phosphotransferase system
    • Abranches, J., Chen, Y.Y. Burne, R.A. (2003) Characterization of Streptococcus mutans strains deficient in EIIAB Man of the sugar phosphotransferase system. Appl Environ Microbiol 69 : 4760 4769.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 4760-4769
    • Abranches, J.1    Chen, Y.Y.2    Burne, R.A.3
  • 2
    • 33744766523 scopus 로고    scopus 로고
    • Different roles of EIIABMan and EIIGlc in regulation of energy metabolism, biofilm development, and competence in Streptococcus mutans
    • Abranches, J., Candella, M.M., Wen, Z.T., Baker, H.V. Burne, R.A. (2006) Different roles of EIIABMan and EIIGlc in regulation of energy metabolism, biofilm development, and competence in Streptococcus mutans. J Bacteriol 188 : 3748 3756.
    • (2006) J Bacteriol , vol.188 , pp. 3748-3756
    • Abranches, J.1    Candella, M.M.2    Wen, Z.T.3    Baker, H.V.4    Burne, R.A.5
  • 4
    • 17644386499 scopus 로고    scopus 로고
    • Role of HtrA in growth and competence of Streptococcus mutans UA159
    • Ahn, S.J., Lemos, J.A. Burne, R.A. (2005) Role of HtrA in growth and competence of Streptococcus mutans UA159. J Bacteriol 187 : 3028 3038.
    • (2005) J Bacteriol , vol.187 , pp. 3028-3038
    • Ahn, S.J.1    Lemos, J.A.2    Burne, R.A.3
  • 5
    • 0031795805 scopus 로고    scopus 로고
    • Transcriptional regulation of the Streptococcus mutans gal operon by the GalR repressor
    • Ajdic, D. Ferretti, J.J. (1998) Transcriptional regulation of the Streptococcus mutans gal operon by the GalR repressor. J Bacteriol 180 : 5727 5732.
    • (1998) J Bacteriol , vol.180 , pp. 5727-5732
    • Ajdic, D.1    Ferretti, J.J.2
  • 6
    • 34447511583 scopus 로고    scopus 로고
    • Global transcriptional analysis of Streptococcus mutans sugar transporters using microarrays
    • Ajdic, D. Pham, V.T. (2007) Global transcriptional analysis of Streptococcus mutans sugar transporters using microarrays. J Bacteriol 189 : 5049 5059.
    • (2007) J Bacteriol , vol.189 , pp. 5049-5059
    • Ajdic, D.1    Pham, V.T.2
  • 7
    • 0030597367 scopus 로고    scopus 로고
    • Organization and nucleotide sequence of the Streptococcus mutans galactose operon
    • Ajdic, D., Sutcliffe, I.C., Russell, R.R. Ferretti, J.J. (1996) Organization and nucleotide sequence of the Streptococcus mutans galactose operon. Gene 180 : 137 144.
    • (1996) Gene , vol.180 , pp. 137-144
    • Ajdic, D.1    Sutcliffe, I.C.2    Russell, R.R.3    Ferretti, J.J.4
  • 9
    • 36148948693 scopus 로고    scopus 로고
    • The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the Group A streptococcus
    • Almengor, A.C., Kinkel, T.L., Day, S.J. McIver, K.S. (2007) The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the Group A streptococcus. J Bacteriol 189 : 8405 8416.
    • (2007) J Bacteriol , vol.189 , pp. 8405-8416
    • Almengor, A.C.1    Kinkel, T.L.2    Day, S.J.3    McIver, K.S.4
  • 10
    • 0023636134 scopus 로고
    • Expression, purification, and characterization of an exo-beta-D- fructosidase of streptococcus mutans
    • Burne, R.A., Schilling, K., Bowen, W.H. Yasbin, R.E. (1987) Expression, purification, and characterization of an exo-beta-D-fructosidase of Streptococcus mutans. J Bacteriol 169 : 4507 4517.
    • (1987) J Bacteriol , vol.169 , pp. 4507-4517
    • Burne, R.A.1    Schilling, K.2    Bowen, W.H.3    Yasbin, R.E.4
  • 11
    • 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., Wen, Z.T., Chen, Y.Y. Penders, J.E. (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
  • 12
    • 85045497108 scopus 로고
    • Mismatch amplification mutation assay (MAMA): Application to the c-H-ras gene
    • Cha, R.S., Zarbl, H., Keohavong, P. Thilly, W.G. (1992) Mismatch amplification mutation assay (MAMA): application to the c-H-ras gene. PCR Methods Appl 2 : 14 20.
    • (1992) PCR Methods Appl , vol.2 , pp. 14-20
    • Cha, R.S.1    Zarbl, H.2    Keohavong, P.3    Thilly, W.G.4
  • 13
    • 0029054845 scopus 로고
    • Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system
    • Cvitkovitch, D.G., Boyd, D.A., Thevenot, T. Hamilton, I.R. (1995) Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system. J Bacteriol 177 : 2251 2258.
    • (1995) J Bacteriol , vol.177 , pp. 2251-2258
    • Cvitkovitch, D.G.1    Boyd, D.A.2    Thevenot, T.3    Hamilton, I.R.4
  • 14
    • 42049092081 scopus 로고    scopus 로고
    • The mechanisms of carbon catabolite repression in bacteria
    • Deutscher, J. (2008) The mechanisms of carbon catabolite repression in bacteria. Curr Opin Microbiol 11 : 87 93.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 87-93
    • Deutscher, J.1
  • 15
    • 0000659321 scopus 로고
    • Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser-HPr and its possible regulatory function
    • Deutscher, J., Kessler, U., Alpert, C.A. Hengstenberg, W. (1984) Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser-HPr and its possible regulatory function. Biochemistry (Wash) 23 : 4455 4460.
    • (1984) Biochemistry (Wash) , vol.23 , pp. 4455-4460
    • Deutscher, J.1    Kessler, U.2    Alpert, C.A.3    Hengstenberg, W.4
  • 16
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., Francke, C. Postma, P.W. (2006) How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol Mol Biol Rev 70 : 939 1031.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 17
    • 1842454273 scopus 로고    scopus 로고
    • Control of expression of the arginine deiminase operon of Streptococcus gordonii by CcpA and Flp
    • Dong, Y., Chen, Y.Y. Burne, R.A. (2004) Control of expression of the arginine deiminase operon of Streptococcus gordonii by CcpA and Flp. J Bacteriol 186 : 2511 2514.
    • (2004) J Bacteriol , vol.186 , pp. 2511-2514
    • Dong, Y.1    Chen, Y.Y.2    Burne, R.A.3
  • 18
    • 0029872740 scopus 로고    scopus 로고
    • Surface location of HPr, a phosphocarrier of the phosphoenolpyruvate: Sugar phosphotransferase system in Streptococcus suis
    • Part
    • Dubreuil, J.D., Jacques, M., Brochu, D., Frenette, M. Vadeboncoeur, C. (1996) Surface location of HPr, a phosphocarrier of the phosphoenolpyruvate: sugar phosphotransferase system in Streptococcus suis. Microbiology 142 (Part 4 837 843.
    • (1996) Microbiology , vol.142 , Issue.4 , pp. 837-843
    • Dubreuil, J.D.1    Jacques, M.2    Brochu, D.3    Frenette, M.4    Vadeboncoeur, C.5
  • 19
    • 0025893868 scopus 로고
    • Improved electroporation and cloning vector system for gram-positive bacteria
    • Dunny, G.M., Lee, L.N. LeBlanc, D.J. (1991) Improved electroporation and cloning vector system for gram-positive bacteria. Appl Environ Microbiol 57 : 1194 1201.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1194-1201
    • Dunny, G.M.1    Lee, L.N.2    Leblanc, D.J.3
  • 20
    • 0030758250 scopus 로고    scopus 로고
    • Replacement of isoleucine-47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine-46
    • Gauthier, M., Brochu, D., Eltis, L.D., Thomas, S. Vadeboncoeur, C. (1997) Replacement of isoleucine-47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine-46. Mol Microbiol 25 : 695 705.
    • (1997) Mol Microbiol , vol.25 , pp. 695-705
    • Gauthier, M.1    Brochu, D.2    Eltis, L.D.3    Thomas, S.4    Vadeboncoeur, C.5
  • 21
    • 0036785653 scopus 로고    scopus 로고
    • Role of RegM, a homologue of the catabolite repressor protein CcpA, in the virulence of Streptococcus pneumoniae
    • Giammarinaro, P. Paton, J.C. (2002) Role of RegM, a homologue of the catabolite repressor protein CcpA, in the virulence of Streptococcus pneumoniae. Infect Immun 70 : 5454 5461.
    • (2002) Infect Immun , vol.70 , pp. 5454-5461
    • Giammarinaro, P.1    Paton, J.C.2
  • 22
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Gorke, B. Stulke, J. (2008) Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol 6 : 613 624.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 613-624
    • Gorke, B.1    Stulke, J.2
  • 23
    • 1542286881 scopus 로고    scopus 로고
    • Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159
    • Griswold, A.R., Chen, Y.Y. Burne, R.A. (2004) Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159. J Bacteriol 186 : 1902 1904.
    • (2004) J Bacteriol , vol.186 , pp. 1902-1904
    • Griswold, A.R.1    Chen, Y.Y.2    Burne, R.A.3
  • 24
    • 31344480412 scopus 로고    scopus 로고
    • Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159
    • Griswold, A.R., Jameson-Lee, M. Burne, R.A. (2006) Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159. J Bacteriol 188 : 834 841.
    • (2006) J Bacteriol , vol.188 , pp. 834-841
    • Griswold, A.R.1    Jameson-Lee, M.2    Burne, R.A.3
  • 25
    • 0027475045 scopus 로고
    • Characterization of a virG mutation that confers constitutive virulence gene expression in Agrobacterium
    • Jin, S., Song, Y., Pan, S.Q. Nester, E.W. (1993) Characterization of a virG mutation that confers constitutive virulence gene expression in Agrobacterium. Mol Microbiol 7 : 555 562.
    • (1993) Mol Microbiol , vol.7 , pp. 555-562
    • Jin, S.1    Song, Y.2    Pan, S.Q.3    Nester, E.W.4
  • 26
    • 0036164801 scopus 로고    scopus 로고
    • PCR ligation mutagenesis in transformable streptococci: Application and efficiency
    • Lau, P.C., Sung, C.K., Lee, J.H., Morrison, D.A. Cvitkovitch, D.G. (2002) PCR ligation mutagenesis in transformable streptococci: application and efficiency. J Microbiol Methods 49 : 193 205.
    • (2002) J Microbiol Methods , vol.49 , pp. 193-205
    • Lau, P.C.1    Sung, C.K.2    Lee, J.H.3    Morrison, D.A.4    Cvitkovitch, D.G.5
  • 27
    • 0018344758 scopus 로고
    • Influence of the lactose plasmid on the metabolism of galactose by Streptococcus lactis
    • LeBlanc, D.J., Crow, V.L., Lee, L.N. Garon, C.F. (1979) Influence of the lactose plasmid on the metabolism of galactose by Streptococcus lactis. J Bacteriol 137 : 878 884.
    • (1979) J Bacteriol , vol.137 , pp. 878-884
    • Leblanc, D.J.1    Crow, V.L.2    Lee, L.N.3    Garon, C.F.4
  • 28
    • 0035421189 scopus 로고    scopus 로고
    • Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism
    • Monedero, V., Poncet, S., Mijakovic, I., Fieulaine, S., Dossonnet, V., Martin-Verstraete, I., et al. (2001) Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism. EMBO J 20 : 3928 3937.
    • (2001) EMBO J , vol.20 , pp. 3928-3937
    • Monedero, V.1    Poncet, S.2    Mijakovic, I.3    Fieulaine, S.4    Dossonnet, V.5    Martin-Verstraete, I.6
  • 29
    • 33644772777 scopus 로고    scopus 로고
    • The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis
    • Muller, W., Horstmann, N., Hillen, W. Sticht, H. (2006) The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis. Febs J 273 : 1251 1261.
    • (2006) Febs J , vol.273 , pp. 1251-1261
    • Muller, W.1    Horstmann, N.2    Hillen, W.3    Sticht, H.4
  • 30
    • 0032502003 scopus 로고    scopus 로고
    • The phosphoenolpyruvate:mannose phosphotransferase system of Streptococcus salivarius. Functional and biochemical characterization of IIABL(Man) and IIABH(Man)
    • Pelletier, M., Lortie, L.A., Frenette, M. Vadeboncoeur, C. (1998) The phosphoenolpyruvate:mannose phosphotransferase system of Streptococcus salivarius. Functional and biochemical characterization of IIABL(Man) and IIABH(Man). Biochemistry 37 : 1604 1612.
    • (1998) Biochemistry , vol.37 , pp. 1604-1612
    • Pelletier, M.1    Lortie, L.A.2    Frenette, M.3    Vadeboncoeur, C.4
  • 31
    • 70350493718 scopus 로고    scopus 로고
    • The transcriptional activator YesS is stimulated by histidine- phosphorylated HPr of the Bacillus subtilis phosphotransferase system
    • Poncet, S., Soret, M., Mervelet, P., Deutscher, J. Noirot, P. (2009) The transcriptional activator YesS is stimulated by histidine-phosphorylated HPr of the Bacillus subtilis phosphotransferase system. J Biol Chem 284 : 28188 28197.
    • (2009) J Biol Chem , vol.284 , pp. 28188-28197
    • Poncet, S.1    Soret, M.2    Mervelet, P.3    Deutscher, J.4    Noirot, P.5
  • 32
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W., Lengeler, J.W. Jacobson, G.R. (1993) Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57 : 543 594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 33
    • 0024451920 scopus 로고
    • Mechanistic and physiological consequences of HPr(ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: Studies with site-specific mutants of HPr
    • Reizer, J., Sutrina, S.L., Saier, M.H., Stewart, G.C., Peterkofsky, A. Reddy, P. (1989) Mechanistic and physiological consequences of HPr(ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: studies with site-specific mutants of HPr. EMBO J 8 : 2111 2120.
    • (1989) EMBO J , vol.8 , pp. 2111-2120
    • Reizer, J.1    Sutrina, S.L.2    Saier, M.H.3    Stewart, G.C.4    Peterkofsky, A.5    Reddy, P.6
  • 34
    • 0026742751 scopus 로고
    • Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans
    • Rosey, E.L. Stewart, G.C. (1992) Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans. J Bacteriol 174 : 6159 6170.
    • (1992) J Bacteriol , vol.174 , pp. 6159-6170
    • Rosey, E.L.1    Stewart, G.C.2
  • 35
    • 0346435105 scopus 로고    scopus 로고
    • Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT
    • Schmalisch, M.H., Bachem, S. Stulke, J. (2003) Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT. J Biol Chem 278 : 51108 51115.
    • (2003) J Biol Chem , vol.278 , pp. 51108-51115
    • Schmalisch, M.H.1    Bachem, S.2    Stulke, J.3
  • 36
    • 0016415604 scopus 로고
    • Chloramphenicol acetyltransferase activity from chloramphenicol-resistant bacteria
    • Shaw, W.V. (1979) Chloramphenicol acetyltransferase activity from chloramphenicol-resistant bacteria. Methods Enzymol 43 : 737 755.
    • (1979) Methods Enzymol , vol.43 , pp. 737-755
    • Shaw, W.V.1
  • 37
    • 40349097955 scopus 로고    scopus 로고
    • A direct link between carbohydrate utilization and virulence in the major human pathogen group A Streptococcus
    • Shelburne, S.A., 3rd., Keith, D., Horstmann, N., Sumby, P., Davenport, M.T., Graviss, E.A., et al. (2008) A direct link between carbohydrate utilization and virulence in the major human pathogen group A Streptococcus. Proc Natl Acad Sci USA 105 : 1698 1703.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1698-1703
    • Shelburne III, S.A.1    Keith, D.2    Horstmann, N.3    Sumby, P.4    Davenport, M.T.5    Graviss, E.A.6
  • 38
    • 0031922267 scopus 로고    scopus 로고
    • Identification of a homolog of CcpA catabolite repressor protein in Streptococcus mutans
    • Simpson, C.L. Russell, R.R. (1998) Identification of a homolog of CcpA catabolite repressor protein in Streptococcus mutans. Infect Immun 66 : 2085 2092.
    • (1998) Infect Immun , vol.66 , pp. 2085-2092
    • Simpson, C.L.1    Russell, R.R.2
  • 39
    • 0030742667 scopus 로고    scopus 로고
    • Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT
    • Stulke, J., Martin-Verstraete, I., Zagorec, M., Rose, M., Klier, A. Rapoport, G. (1997) Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT. Mol Microbiol 25 : 65 78.
    • (1997) Mol Microbiol , vol.25 , pp. 65-78
    • Stulke, J.1    Martin-Verstraete, I.2    Zagorec, M.3    Rose, M.4    Klier, A.5    Rapoport, G.6
  • 40
    • 0027478535 scopus 로고
    • Identification of Streptococcus mutans antigen D as the HPr component of the sugar-phosphotransferase transport system
    • Sutcliffe, I.C., Hogg, S.D. Russell, R.R. (1993) Identification of Streptococcus mutans antigen D as the HPr component of the sugar- phosphotransferase transport system. FEMS Microbiol Lett 107 : 67 70.
    • (1993) FEMS Microbiol Lett , vol.107 , pp. 67-70
    • Sutcliffe, I.C.1    Hogg, S.D.2    Russell, R.R.3
  • 41
    • 0029010316 scopus 로고
    • Regulation of ATP-dependent P-(Ser)-HPr formation in Streptococcus mutans and Streptococcus salivarius
    • Thevenot, T., Brochu, D., Vadeboncoeur, C. Hamilton, I.R. (1995) Regulation of ATP-dependent P-(Ser)-HPr formation in Streptococcus mutans and Streptococcus salivarius. J Bacteriol 177 : 2751 2759.
    • (1995) J Bacteriol , vol.177 , pp. 2751-2759
    • Thevenot, T.1    Brochu, D.2    Vadeboncoeur, C.3    Hamilton, I.R.4
  • 42
    • 0035695915 scopus 로고    scopus 로고
    • Structural insights into the regulation of bacterial signalling proteins containing PRDs
    • van Tilbeurgh, H. Declerck, N. (2001) Structural insights into the regulation of bacterial signalling proteins containing PRDs. Curr Opin Struct Biol 11 : 685 693.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 685-693
    • Van Tilbeurgh, H.1    Declerck, N.2
  • 43
    • 0031031808 scopus 로고    scopus 로고
    • The phosphoenolpyruvate:sugar phosphotransferase system of oral streptococci and its role in the control of sugar metabolism
    • Vadeboncoeur, C. Pelletier, M. (1997) The phosphoenolpyruvate:sugar phosphotransferase system of oral streptococci and its role in the control of sugar metabolism. FEMS Microbiol Rev 19 : 187 207.
    • (1997) FEMS Microbiol Rev , vol.19 , pp. 187-207
    • Vadeboncoeur, C.1    Pelletier, M.2
  • 44
    • 0036135464 scopus 로고    scopus 로고
    • Analysis of cis- and trans-acting factors involved in regulation of the Streptococcus mutans fructanase gene (fruA)
    • Wen, Z.T. Burne, R.A. (2002) Analysis of cis- and trans-acting factors involved in regulation of the Streptococcus mutans fructanase gene (fruA). J Bacteriol 184 : 126 133.
    • (2002) J Bacteriol , vol.184 , pp. 126-133
    • Wen, Z.T.1    Burne, R.A.2
  • 45
    • 51649120143 scopus 로고    scopus 로고
    • Multiple sugar: Phosphotransferase system permeases participate in catabolite modification of gene expression in Streptococcus mutans
    • Zeng, L. Burne, R.A. (2008) Multiple sugar: phosphotransferase system permeases participate in catabolite modification of gene expression in Streptococcus mutans. Mol Microbiol 70 : 197 208.
    • (2008) Mol Microbiol , vol.70 , pp. 197-208
    • Zeng, L.1    Burne, R.A.2
  • 46
    • 64049112629 scopus 로고    scopus 로고
    • Transcriptional regulation of the cellobiose operon of Streptococcus mutans
    • Zeng, L. Burne, R.A. (2009) Transcriptional regulation of the cellobiose operon of Streptococcus mutans. J Bacteriol 191 : 2153 2162.
    • (2009) J Bacteriol , vol.191 , pp. 2153-2162
    • Zeng, L.1    Burne, R.A.2
  • 47
    • 33748662003 scopus 로고    scopus 로고
    • A novel signal transduction system and feedback loop regulate fructan hydrolase gene expression in Streptococcus mutans
    • Zeng, L., Wen, Z.T. Burne, R.A. (2006a) A novel signal transduction system and feedback loop regulate fructan hydrolase gene expression in Streptococcus mutans. Mol Microbiol 62 : 187 200.
    • (2006) Mol Microbiol , vol.62 , pp. 187-200
    • Zeng, L.1    Wen, Z.T.2    Burne, R.A.3
  • 48
    • 31344444145 scopus 로고    scopus 로고
    • Characterization of cis-acting sites controlling arginine deiminase gene expression in Streptococcus gordonii
    • Zeng, L., Dong, Y. Burne, R.A. (2006b) Characterization of cis-acting sites controlling arginine deiminase gene expression in Streptococcus gordonii. J Bacteriol 188 : 941 949.
    • (2006) J Bacteriol , vol.188 , pp. 941-949
    • Zeng, L.1    Dong, Y.2    Burne, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.