메뉴 건너뛰기




Volumn 29, Issue 3, 2010, Pages 297-304

The influence of HtrA expression on the growth of streptococcus mutans during acid stress

Author keywords

Acid; HtrA; Korean; Streptococcus mutans; Stress

Indexed keywords

BACTERIAL PROTEIN; ERYTHROMYCIN; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASEB; GLUCURONOSYLTRANSFERASEC; HIGH TEMPERATURE REQUIREMENT A PROTEIN; KANAMYCIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77953481138     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10059-010-0036-9     Document Type: Article
Times cited : (10)

References (31)
  • 1
    • 17644386499 scopus 로고    scopus 로고
    • Role of HtrA in growth and competence of Streptococcus mutans UA159
    • Ahn, S.J., Lemos, J.A., and 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
  • 2
    • 33644780749 scopus 로고    scopus 로고
    • Multilevel control of competence development and stress tolerance in Streptococcus mutans UA159
    • Ahn, S. J., Wen, Z.T., and Burne, R.A. (2006). Multilevel control of competence development and stress tolerance in Streptococcus mutans UA159. Infect. Immun. 74, 1631-1642.
    • (2006) Infect. Immun. , vol.74 , pp. 1631-1642
    • Ahn, S.J.1    Wen, Z.T.2    Burne, R.A.3
  • 4
    • 42049092059 scopus 로고    scopus 로고
    • Markerless multiple-genedeletion system for Streptococcus mutans
    • Banerjee, A., and Biswas, I. (2008). Markerless multiple-genedeletion system for Streptococcus mutans. Appl. Environ. Microbiol. 74, 2037-2042.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 2037-2042
    • Banerjee, A.1    Biswas, I.2
  • 5
    • 25444479087 scopus 로고    scopus 로고
    • Role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans
    • Biswas, S., and Biswas, I. (2005). Role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans. Infect. Immun. 73, 6923-6934.
    • (2005) Infect. Immun. , vol.73 , pp. 6923-6934
    • Biswas, S.1    Biswas, I.2
  • 6
    • 0033812734 scopus 로고    scopus 로고
    • Improved vectors for nisin-controlled expression in gram-positive bacteria
    • Bryan, E.M., Bae, T., Kleerebezem, M., and Dunny, G.M. (2000). Improved vectors for nisin-controlled expression in gram-positive bacteria. Plasmid 44, 183-190.
    • (2000) Plasmid , vol.44 , pp. 183-190
    • Bryan, E.M.1    Bae, T.2    Kleerebezem, M.3    Dunny, G.M.4
  • 7
    • 34548569994 scopus 로고    scopus 로고
    • The adaptive response of Streptococcus mutans towards oral care products: Involvement of the ClpP serine protease
    • Deng, D.M., ten Cate, J.M., and Crielaard, W. (2007). The adaptive response of Streptococcus mutans towards oral care products: involvement of the ClpP serine protease. Eur. J. Oral Sci. 115, 363-370.
    • (2007) Eur. J. Oral Sci. , vol.115 , pp. 363-370
    • Deng, D.M.1    Ten Cate, J.M.2    Crielaard, W.3
  • 8
    • 0029908161 scopus 로고    scopus 로고
    • The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes
    • Elzer, P.H., Phillips, R.W., Robertson, G.T., and Roop, R.M., 2nd. (1996). The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes. Infect. Immun. 64, 4838-4841.
    • (1996) Infect. Immun. , vol.64 , pp. 4838-4841
    • Elzer, P.H.1    Phillips, R.W.2    Robertson, G.T.3    Roop II, R.M.4
  • 9
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. (2003). Proteolysis in bacterial regulatory circuits. Annu. Rev. Cell Dev. Biol. 19, 565-587.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 10
    • 2542617706 scopus 로고    scopus 로고
    • Role of HtrA in the virulence and competence of Streptococcus pneumoniae
    • Ibrahim, Y.M., Kerr, A.R., McCluskey, J., and Mitchell, T.J. (2004). Role of HtrA in the virulence and competence of Streptococcus pneumoniae. Infect. Immun. 72, 3584-3591.
    • (2004) Infect. Immun. , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1    Kerr, A.R.2    McCluskey, J.3    Mitchell, T.J.4
  • 12
    • 0034868619 scopus 로고    scopus 로고
    • Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
    • Jones, C.H., Bolken, T.C., Jones, K.F., Zeller, G.O., and Hruby, D.E. (2001). Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes. Infect. Immun. 69, 5538-5545.
    • (2001) Infect. Immun. , vol.69 , pp. 5538-5545
    • Jones, C.H.1    Bolken, T.C.2    Jones, K.F.3    Zeller, G.O.4    Hruby, D.E.5
  • 13
    • 77953493289 scopus 로고    scopus 로고
    • Isolation and characterization of the Streptococcus mutans from Korean children with caries
    • Kang, K.H., Kim, J.Y., Nam, J.S., and Jin, I. (2007). Isolation and characterization of the Streptococcus mutans from Korean children with caries. J. Exp. Biomed. Sci. 13, 341-347.
    • (2007) J. Exp. Biomed. Sci. , vol.13 , pp. 341-347
    • Kang, K.H.1    Kim, J.Y.2    Nam, J.S.3    Jin, I.4
  • 14
    • 40049107314 scopus 로고    scopus 로고
    • The mechanism of temperature-induced bacterial HtrA activation
    • Kim, D.Y., Kwon, E., Shin, Y.K., Kweon, D.H., and Kim, K.K. (2008). The mechanism of temperature-induced bacterial HtrA activation. J. Mol. Biol. 377, 410-420.
    • (2008) J. Mol. Biol. , vol.377 , pp. 410-420
    • Kim, D.Y.1    Kwon, E.2    Shin, Y.K.3    Kweon, D.H.4    Kim, K.K.5
  • 15
    • 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., and 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
  • 16
    • 0028264805 scopus 로고
    • A low-pH-inducible, stationary phase acid tolerance response in Salmonella typhimurium
    • Lee, I.S., Slonczwski, J.L., and Foster, J.W. (1994). A low-pH-inducible, stationary phase acid tolerance response in Salmonella typhimurium. J. Bacteriol. 176, 1422-1426.
    • (1994) J. Bacteriol. , vol.176 , pp. 1422-1426
    • Lee, I.S.1    Slonczwski, J.L.2    Foster, J.W.3
  • 17
    • 44949255004 scopus 로고    scopus 로고
    • Expressed Sequence Tag Analysis of Antarctic Hairgrass Deschampsia antarctica from King George Island, Antarctica
    • Lee, H., Cho, H.H., Kim, I.C., Yim, J.H., Lee, H.K., and Lee, Y.K. (2008). Expressed Sequence Tag Analysis of Antarctic Hairgrass Deschampsia antarctica from King George Island, Antarctica. Mol. Cells 25, 258-264.
    • (2008) Mol. Cells , vol.25 , pp. 258-264
    • Lee, H.1    Cho, H.H.2    Kim, I.C.3    Yim, J.H.4    Lee, H.K.5    Lee, Y.K.6
  • 18
    • 2942625671 scopus 로고    scopus 로고
    • Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance
    • Len, A.C., Harty, D.W., and Jacques, N.A. (2004). Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance. Microb. 150, 1339-1351.
    • (2004) Microb. , vol.150 , pp. 1339-1351
    • Len, A.C.1    Harty, D.W.2    Jacques, N.A.3
  • 19
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska, B., Fayet, O., Baird, L., and Georgopoulos, C. (1989). Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171, 1574-1584.
    • (1989) J. Bacteriol. , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 20
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real time quantitave PCR and the 2-ΔΔct method
    • Livak, K.J., and Schmitteng, T.D. (2001). Analysis of relative gene expression data using real time quantitave PCR and the 2-ΔΔct method. Methods 25, 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmitteng, T.D.2
  • 21
    • 0026746484 scopus 로고
    • Microbiological aspects of the chemical control of plaque and gingivitis
    • Marsh, P.D. (1992). Microbiological aspects of the chemical control of plaque and gingivitis. J. Dent. Res. 71, 1431-1438.
    • (1992) J. Dent. Res. , vol.71 , pp. 1431-1438
    • Marsh, P.D.1
  • 22
    • 0037432698 scopus 로고    scopus 로고
    • Acid tolerance response of biofilm cells of Streptococcus mutans
    • Mcneill, K., and Hamilton, I.R. (2003). Acid tolerance response of biofilm cells of Streptococcus mutans. FEMS Microbiol. Lett. 221, 25-30.
    • (2003) FEMS Microbiol. Lett. , vol.221 , pp. 25-30
    • Mcneill, K.1    Hamilton, I.R.2
  • 23
    • 0034740734 scopus 로고    scopus 로고
    • Contributions of three glycosyltransferases to sucrose-dependent adherence of Streptococcus mutans
    • Ooshima, T., Matsumura, M., Hoshino, T., Kawabata, S., Sobue, S., and Fujiwara, T. (2001). Contributions of three glycosyltransferases to sucrose-dependent adherence of Streptococcus mutans. J. Dent. Res. 80, 1672-1677.
    • (2001) J. Dent. Res. , vol.80 , pp. 1672-1677
    • Ooshima, T.1    Matsumura, M.2    Hoshino, T.3    Kawabata, S.4    Sobue, S.5    Fujiwara, T.6
  • 24
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M.J., and Wren, B.W. (1997). The HtrA family of serine proteases. Mol. Microbiol. 26, 209-221.
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 25
    • 0032805531 scopus 로고    scopus 로고
    • PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease
    • Sassoon, N., Arié, J.P., and Betton, J.M. (1999). PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease. Mol. Microbiol. 33, 583-589.
    • (1999) Mol. Microbiol. , vol.33 , pp. 583-589
    • Sassoon, N.1    Arié, J.P.2    Betton, J.M.3
  • 26
    • 0029156237 scopus 로고
    • Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures
    • Skórko-Glonek, J., Wawrzynów, A., Krzewski, K., Kurpierz, K., and Lipińska, B. (1995). Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures. Gene 163, 47-52.
    • (1995) Gene , vol.163 , pp. 47-52
    • Skórko-Glonek, J.1    Wawrzynów, A.2    Krzewski, K.3    Kurpierz, K.4    Lipińska, B.5
  • 27
    • 23744437997 scopus 로고    scopus 로고
    • Role for HtrA in stress induction and virulence potential in Listeria monocytogenes
    • Stack, H.M., Sleator, R.D., Bowers, M., Hill, C., and Gahan, C.G. (2005). Role for HtrA in stress induction and virulence potential in Listeria monocytogenes. Appl. Environ. Microbiol. 71, 4241-4247.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4241-4247
    • Stack, H.M.1    Sleator, R.D.2    Bowers, M.3    Hill, C.4    Gahan, C.G.5
  • 28
    • 0028043858 scopus 로고
    • Cloning, characterization and construction of htrA and htrA-like mutants of Brucella abortus and their survival in BALB/c mice
    • Tatum, F.M., Cheville, N.F., and Morfitt, D. (1994). Cloning, characterization and construction of htrA and htrA-like mutants of Brucella abortus and their survival in BALB/c mice. Microb. Pathog. 17, 23-36.
    • (1994) Microb. Pathog. , vol.17 , pp. 23-36
    • Tatum, F.M.1    Cheville, N.F.2    Morfitt, D.3
  • 29
    • 0029248054 scopus 로고
    • Xylital: A review of its action on Mutans streptococci and dental plaque-its clinical significance
    • Trahan, L. (1995). Xylital: a review of its action on Mutans streptococci and dental plaque-its clinical significance. Int. Dent. J. 45, 77-92.
    • (1995) Int. Dent. J. , vol.45 , pp. 77-92
    • Trahan, L.1
  • 31
    • 27244444906 scopus 로고    scopus 로고
    • Biochemical analysis of a cytosolic small heat shock protein, NtHSP18.3, from Nicotiana tabacum
    • Yu, J.H., Kim, K.P., Park, S.M., and Hong, C.B. (2005). Biochemical analysis of a cytosolic small heat shock protein, NtHSP18.3, from Nicotiana tabacum. Mol. Cells 19, 328-333.
    • (2005) Mol. Cells , vol.19 , pp. 328-333
    • Yu, J.H.1    Kim, K.P.2    Park, S.M.3    Hong, C.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.