메뉴 건너뛰기




Volumn 188, Issue 19, 2006, Pages 6877-6888

The atlA operon of Streptococcus mutans: Role in autolysin maturation and cell surface biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ADHESIN P1; AUTOLYSIN; BACTERIAL PROTEIN; DODECYL SULFATE SODIUM; MEMBRANE PROTEIN; PROTEIN; PROTEIN ATLA; PROTEIN DERIVATIVE; PROTEIN SMU0630; PROTEIN THMA; REPETITIVE DNA; UNCLASSIFIED DRUG;

EID: 33749343266     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00536-06     Document Type: Article
Times cited : (66)

References (90)
  • 1
    • 17644386499 scopus 로고    scopus 로고
    • Role of HtrA in growth and competence of Streptococcus mutans UA159
    • Ahn, S. J., J. A. Lemos, and R. A. Burne. 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., Z. T. Wen, and R. A. Burne. 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
  • 3
    • 0031855362 scopus 로고    scopus 로고
    • Development of competence in Streptococcus pneumoniae: Pheromone autoinduction and control of quorum sensing by the oligopeptide permease
    • Alloing, G., B. Martin, C. Granadel, and J. P. Claverys. 1998. Development of competence in Streptococcus pneumoniae: pheromone autoinduction and control of quorum sensing by the oligopeptide permease. Mol. Microbiol. 29:75-83.
    • (1998) Mol. Microbiol. , vol.29 , pp. 75-83
    • Alloing, G.1    Martin, B.2    Granadel, C.3    Claverys, J.P.4
  • 4
    • 0023199712 scopus 로고
    • Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci
    • Ayakawa, G. Y., L. W. Boushell, P. J. Crowley, G. W. Erdos, W. P. McArthur, and A. S. Bleiweis. 1987. Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci. Infect. Immun. 55:2759-2767.
    • (1987) Infect. Immun. , vol.55 , pp. 2759-2767
    • Ayakawa, G.Y.1    Boushell, L.W.2    Crowley, P.J.3    Erdos, G.W.4    McArthur, W.P.5    Bleiweis, A.S.6
  • 5
    • 0031964736 scopus 로고    scopus 로고
    • Pleiotropic mutations alter the kinetics of calcium transport, competence regulation, autolysis and experimental virulence in Streptococcus pneumoniae
    • Azoulay-Dupuis, E., V. Rieux, C. Rivier, and M. C. Trombe. 1998. Pleiotropic mutations alter the kinetics of calcium transport, competence regulation, autolysis and experimental virulence in Streptococcus pneumoniae. Res. Microbiol. 149:5-13.
    • (1998) Res. Microbiol. , vol.149 , pp. 5-13
    • Azoulay-Dupuis, E.1    Rieux, V.2    Rivier, C.3    Trombe, M.C.4
  • 6
    • 0032541330 scopus 로고    scopus 로고
    • Targeting of muralytic enzymes to the cell division site of gram-positive bacteria: Repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus
    • Baba, T., and O. Schneewind. 1998. Targeting of muralytic enzymes to the cell division site of gram-positive bacteria: repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus. EMBO J. 17:4639-4646.
    • (1998) EMBO J. , vol.17 , pp. 4639-4646
    • Baba, T.1    Schneewind, O.2
  • 7
    • 0027491818 scopus 로고
    • Cloning and molecular analysis of genes affecting expression of binding substance, the recipient-encoded receptor(s) mediating mating aggregate formation in Enterococcus faecalis
    • Bensing, B. A., and G. M. Dunny. 1993. Cloning and molecular analysis of genes affecting expression of binding substance, the recipient-encoded receptor(s) mediating mating aggregate formation in Enterococcus faecalis. J. Bacteriol. 175:7421-7429.
    • (1993) J. Bacteriol. , vol.175 , pp. 7421-7429
    • Bensing, B.A.1    Dunny, G.M.2
  • 8
    • 0024322485 scopus 로고
    • Contribution of autolysin to virulence of Streptococcus pneumoniae
    • Berry, A. M., R. A. Lock, D. Hansman, and J. C. Paton. 1989. Contribution of autolysin to virulence of Streptococcus pneumoniae. Infect. Immun. 57: 2324-2330.
    • (1989) Infect. Immun. , vol.57 , pp. 2324-2330
    • Berry, A.M.1    Lock, R.A.2    Hansman, D.3    Paton, J.C.4
  • 9
    • 0031963480 scopus 로고    scopus 로고
    • The role of autolysins during vegetative growth of Bacillus subtilis 168
    • Blackman, S. A., T. J. Smith, and S. J. Foster. 1998. The role of autolysins during vegetative growth of Bacillus subtilis 168. Microbiology 144:73-82.
    • (1998) Microbiology , vol.144 , pp. 73-82
    • Blackman, S.A.1    Smith, T.J.2    Foster, S.J.3
  • 10
    • 17644388851 scopus 로고    scopus 로고
    • A hypothetical protein of Streptococcus mutans is critical for biofilm formation
    • Brown, T. A., Jr., S. J. Ahn, R. N. Frank, Y. Y. Chen, J. A. Lemos, and R. A. Burne. 2005. A hypothetical protein of Streptococcus mutans is critical for biofilm formation. Infect. Immun. 73:3147-3151.
    • (2005) Infect. Immun. , vol.73 , pp. 3147-3151
    • Brown Jr., T.A.1    Ahn, S.J.2    Frank, R.N.3    Chen, Y.Y.4    Lemos, J.A.5    Burne, R.A.6
  • 11
    • 0030814446 scopus 로고    scopus 로고
    • Autolysis of Lactococcus lactis caused by induced overproduction of its major autolysin, AcmA
    • Buist, G., H. Karsens, A. Nauta, D. van Sinderen, G. Venema, and J. Kok. 1997. Autolysis of Lactococcus lactis caused by induced overproduction of its major autolysin, AcmA. Appl. Environ. Microbiol. 63:2722-2728.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2722-2728
    • Buist, G.1    Karsens, H.2    Nauta, A.3    Van Sinderen, D.4    Venema, G.5    Kok, J.6
  • 12
    • 0031766710 scopus 로고    scopus 로고
    • Autolysis of Lactococcus lactis is influenced by proteolysis
    • Buist, G., G. Venema, and J. Kok. 1998. Autolysis of Lactococcus lactis is influenced by proteolysis. J. Bacteriol. 180:5947-5953.
    • (1998) J. Bacteriol. , vol.180 , pp. 5947-5953
    • Buist, G.1    Venema, G.2    Kok, J.3
  • 13
    • 0031768170 scopus 로고    scopus 로고
    • Transcriptional regulation of the Streptococcus salivarius 57.1 urease operon
    • Chen, Y. Y., C. A. Weaver, D. R. Mendelsohn, and R. A. Burne. 1998. Transcriptional regulation of the Streptococcus salivarius 57.1 urease operon. J. Bacteriol. 180:5769-5775.
    • (1998) J. Bacteriol. , vol.180 , pp. 5769-5775
    • Chen, Y.Y.1    Weaver, C.A.2    Mendelsohn, D.R.3    Burne, R.A.4
  • 14
    • 0034777402 scopus 로고    scopus 로고
    • A 60-kilodalton immunodominant glycoprotein is essential for cell wall integrity and the maintenance of cell shape in Streptococcus mutans
    • Chia, J. S., L. Y. Chang, C. T. Shun, Y. Y. Chang, Y. G. Tsay, and J. Y. Chen. 2001. A 60-kilodalton immunodominant glycoprotein is essential for cell wall integrity and the maintenance of cell shape in Streptococcus mutans. Infect. Immun. 69:6987-6998.
    • (2001) Infect. Immun. , vol.69 , pp. 6987-6998
    • Chia, J.S.1    Chang, L.Y.2    Shun, C.T.3    Chang, Y.Y.4    Tsay, Y.G.5    Chen, J.Y.6
  • 15
    • 0017870993 scopus 로고
    • Autolytic defective mutant of Streptococcus faecalis
    • Cornett, J. B., B. E. Redman, and G. D. Shockman. 1978. Autolytic defective mutant of Streptococcus faecalis. J. Bacteriol. 133:631-640.
    • (1978) J. Bacteriol. , vol.133 , pp. 631-640
    • Cornett, J.B.1    Redman, B.E.2    Shockman, G.D.3
  • 16
    • 0018194284 scopus 로고
    • Cellular lysis of Streptococcus faecalis induced with triton X-100
    • Cornett, J. B., and G. D. Shockman. 1978. Cellular lysis of Streptococcus faecalis induced with triton X-100. J. Bacteriol. 135:153-160.
    • (1978) J. Bacteriol. , vol.135 , pp. 153-160
    • Cornett, J.B.1    Shockman, G.D.2
  • 17
    • 1442349821 scopus 로고    scopus 로고
    • Interconnection of competence, stress and CiaR regulons in Streptococcus pneumoniae: Competence triggers stationary phase autolysis of ciaR mutant cells
    • Dagkessamanskaia, A., M. Moscoso, V. Henard, S. Guiral, K. Overweg, M. Reuter, B. Martin, J. Wells, and J. P. Claverys. 2004. Interconnection of competence, stress and CiaR regulons in Streptococcus pneumoniae: competence triggers stationary phase autolysis of ciaR mutant cells. Mol. Microbiol. 51:1071-1086.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1071-1086
    • Dagkessamanskaia, A.1    Moscoso, M.2    Henard, V.3    Guiral, S.4    Overweg, K.5    Reuter, M.6    Martin, B.7    Wells, J.8    Claverys, J.P.9
  • 18
    • 0026786136 scopus 로고
    • Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae
    • Diaz, E., R. Lopez, and J. L. Garcia. 1992. Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae. J. Bacteriol. 174:5508-5515.
    • (1992) J. Bacteriol. , vol.174 , pp. 5508-5515
    • Diaz, E.1    Lopez, R.2    Garcia, J.L.3
  • 19
    • 0029617205 scopus 로고
    • Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4
    • Foster, S. J. 1995. Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4. J. Bacteriol. 177:5723-5725.
    • (1995) J. Bacteriol. , vol.177 , pp. 5723-5725
    • Foster, S.J.1
  • 21
    • 0032871131 scopus 로고    scopus 로고
    • Genetic and physiological studies of the CiaH-CiaR two-component signal-transducing system involved in cefotaxime resistance and competence of Streptococcus pneumoniae
    • Giammarinaro, P., M. Sicard, and A. M. Gasc. 1999. Genetic and physiological studies of the CiaH-CiaR two-component signal-transducing system involved in cefotaxime resistance and competence of Streptococcus pneumoniae. Microbiology 145:1859-1869.
    • (1999) Microbiology , vol.145 , pp. 1859-1869
    • Giammarinaro, P.1    Sicard, M.2    Gasc, A.M.3
  • 22
    • 0034508719 scopus 로고    scopus 로고
    • Varying influence of the autolysin, N-acetyl muramidase, and the cell envelope proteinase on the rate of autolysis of six commercial Lactococcus lactis cheese starter bacteria grown in milk
    • Govindasamy-Lucey, S., P. K. Gopal, P. A. Sullivan, and C. J. Pillidge. 2000. Varying influence of the autolysin, N-acetyl muramidase, and the cell envelope proteinase on the rate of autolysis of six commercial Lactococcus lactis cheese starter bacteria grown in milk. J. Dairy Res. 67:585-596.
    • (2000) J. Dairy Res. , vol.67 , pp. 585-596
    • Govindasamy-Lucey, S.1    Gopal, P.K.2    Sullivan, P.A.3    Pillidge, C.J.4
  • 23
    • 0034065895 scopus 로고    scopus 로고
    • The Staphylococcus aureus IrgAB operon modulates murein hydrolase activity and penicillin tolerance
    • Groicher, K. H., B. A. Firek, D. F. Fujimoto, and K. W. Bayles. 2000. The Staphylococcus aureus IrgAB operon modulates murein hydrolase activity and penicillin tolerance. J. Bacteriol. 182:1794-1801.
    • (2000) J. Bacteriol. , vol.182 , pp. 1794-1801
    • Groicher, K.H.1    Firek, B.A.2    Fujimoto, D.F.3    Bayles, K.W.4
  • 24
    • 32244441319 scopus 로고    scopus 로고
    • Inhibition of competence development in Streptococcus pneumoniae by increased basal-level expression of the ComDE two-component regulatory system
    • Guiral, S., V. Henard, C. Granadel, B. Martin, and J. P. Claverys. 2006. Inhibition of competence development in Streptococcus pneumoniae by increased basal-level expression of the ComDE two-component regulatory system. Microbiology 152:323-331.
    • (2006) Microbiology , vol.152 , pp. 323-331
    • Guiral, S.1    Henard, V.2    Granadel, C.3    Martin, B.4    Claverys, J.P.5
  • 25
    • 0029152281 scopus 로고
    • Mutational analysis of the putative leukotoxin transport genes in Actinobacillus actinomycetemcomitans
    • Guthmiller, J. M., D. Kolodrubetz, and E. Kraig. 1995. Mutational analysis of the putative leukotoxin transport genes in Actinobacillus actinomycetemcomitans. Microb. Pathog. 18:307-321.
    • (1995) Microb. Pathog. , vol.18 , pp. 307-321
    • Guthmiller, J.M.1    Kolodrubetz, D.2    Kraig, E.3
  • 26
    • 0031663963 scopus 로고    scopus 로고
    • Identification of a competence regulon in Streptococcus pneumoniae by genomic analysis
    • Havarstein, L. S. 1998. Identification of a competence regulon in Streptococcus pneumoniae by genomic analysis. Trends Microbiol. 6:297-300.
    • (1998) Trends Microbiol. , vol.6 , pp. 297-300
    • Havarstein, L.S.1
  • 27
    • 0030668266 scopus 로고    scopus 로고
    • Natural competence in the genus Streptococcus: Evidence that streptococci can change phenotype by interspecies recombinational exchanges
    • Havarstein, L. S., R. Hakenbeck, and P. Gaustad. 1997. Natural competence in the genus Streptococcus: evidence that streptococci can change phenotype by interspecies recombinational exchanges. J. Bacteriol. 179:6589-6594.
    • (1997) J. Bacteriol. , vol.179 , pp. 6589-6594
    • Havarstein, L.S.1    Hakenbeck, R.2    Gaustad, P.3
  • 28
    • 0030798156 scopus 로고    scopus 로고
    • Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface
    • Heilmann, C., M. Hussain, G. Peters, and F. Gotz. 1997. Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface. Mol. Microbiol. 24:1013-1024.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1013-1024
    • Heilmann, C.1    Hussain, M.2    Peters, G.3    Gotz, F.4
  • 29
    • 0024580287 scopus 로고
    • DNA sequence of the Pasteurella haemolytica leukotoxin gene cluster
    • Highlander, S. K., M. Chidambaram, M. J. Engler, and G. M. Weinstock. 1989. DNA sequence of the Pasteurella haemolytica leukotoxin gene cluster. DNA. 8:15-28.
    • (1989) DNA , vol.8 , pp. 15-28
    • Highlander, S.K.1    Chidambaram, M.2    Engler, M.J.3    Weinstock, G.M.4
  • 30
    • 0025357078 scopus 로고
    • Secretion and expression of the Pasteurella haemolytica Leukotoxin
    • Highlander, S. K., M. J. Engler, and G. M. Weinstock. 1990. Secretion and expression of the Pasteurella haemolytica Leukotoxin. J. Bacteriol. 172:2343-2350.
    • (1990) J. Bacteriol. , vol.172 , pp. 2343-2350
    • Highlander, S.K.1    Engler, M.J.2    Weinstock, G.M.3
  • 31
    • 0028825333 scopus 로고
    • From growth to autolysis: The murein hydrolases in Escherichia coli
    • Holtje, J. V. 1995. From growth to autolysis: the murein hydrolases in Escherichia coli. Arch. Microbiol. 164:243-254.
    • (1995) Arch. Microbiol. , vol.164 , pp. 243-254
    • Holtje, J.V.1
  • 32
    • 0022001167 scopus 로고
    • Competence-specific autolysis in Streptococcus sanguis
    • Horne, D., and A. Tomasz. 1985. Competence-specific autolysis in Streptococcus sanguis. J. Gen. Microbiol. 131:533-541.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 533-541
    • Horne, D.1    Tomasz, A.2
  • 33
    • 0038052201 scopus 로고    scopus 로고
    • Effect of calcium on adherence of Streptococcus mutans MT6R(serotype c) surface protein P1
    • In Chinese
    • Huang, D., Z. Luo, and X. Zhou. 2000. Effect of calcium on adherence of Streptococcus mutans MT6R(serotype c) surface protein P1. Hua Xi Kou Qiang Yi Xue Za Zhi 18:163-164, 180. [In Chinese.]
    • (2000) Hua Xi Kou Qiang Yi Xue Za Zhi , vol.18 , pp. 163-164
    • Huang, D.1    Luo, Z.2    Zhou, X.3
  • 35
    • 0031978461 scopus 로고    scopus 로고
    • Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis
    • Ishikawa, S., Y. Hara, R. Ohnishi, and J. Sekiguchi. 1998. Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis. J. Bacteriol. 180:2549-2555.
    • (1998) J. Bacteriol. , vol.180 , pp. 2549-2555
    • Ishikawa, S.1    Hara, Y.2    Ohnishi, R.3    Sekiguchi, J.4
  • 37
    • 0025824740 scopus 로고
    • Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene
    • Kuroda, A., and J. Sekiguchi. 1991. Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene. J. Bacteriol. 173:7304-7312.
    • (1991) J. Bacteriol. , vol.173 , pp. 7304-7312
    • Kuroda, A.1    Sekiguchi, J.2
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 39
    • 0026673165 scopus 로고
    • Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L- alanine amidase and its modifier
    • Lazarevic, V., P. Margot, B. Soldo, and D. Karamata. 1992. Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier. J. Gen. Microbiol. 138:1949-1961.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1949-1961
    • Lazarevic, V.1    Margot, P.2    Soldo, B.3    Karamata, D.4
  • 40
    • 0026782639 scopus 로고
    • Molecular, genetic, and functional analysis of the basic replicon of pVA380-1, a plasmid of oral streptococcal origin
    • LeBlanc, D. J., L. N. Lee, and A. Abu-Al-Jaibat. 1992. Molecular, genetic, and functional analysis of the basic replicon of pVA380-1, a plasmid of oral streptococcal origin. Plasmid 28:130-145.
    • (1992) Plasmid , vol.28 , pp. 130-145
    • LeBlanc, D.J.1    Lee, L.N.2    Abu-Al-Jaibat, A.3
  • 41
    • 0037305827 scopus 로고    scopus 로고
    • Roles of sortase in surface expression of the major protein adhesin P1, saliva-induced aggregation and adherence, and cariogenicity of Streptococcus mutatis
    • Lee, S. F., and T. L. Boran. 2003. Roles of sortase in surface expression of the major protein adhesin P1, saliva-induced aggregation and adherence, and cariogenicity of Streptococcus mutatis. Infect. Immun. 71:676-681.
    • (2003) Infect. Immun. , vol.71 , pp. 676-681
    • Lee, S.F.1    Boran, T.L.2
  • 42
    • 0023819738 scopus 로고
    • Molecular cloning and expression of a Streptococcus mutans major surface protein antigen, P1 (I/II), in Escherichia coli
    • Lee, S. F., A. Progulske-Fox, and A. S. Bleiweis. 1988. Molecular cloning and expression of a Streptococcus mutans major surface protein antigen, P1 (I/II), in Escherichia coli. Infect. Immun. 56:2114-2119.
    • (1988) Infect. Immun. , vol.56 , pp. 2114-2119
    • Lee, S.F.1    Progulske-Fox, A.2    Bleiweis, A.S.3
  • 43
    • 0024443982 scopus 로고
    • Construction and characterization of isogenic mutants of Streptococcus mutans deficient in major surface protein antigen P1 (I/II)
    • Lee, S. F., A. Progulske-Fox, G. W. Erdos, D. A. Piacentini, G. Y. Ayakawa, P. J. Crowley, and A. S. Bleiweis. 1989. Construction and characterization of isogenic mutants of Streptococcus mutans deficient in major surface protein antigen P1 (I/II). Infect. Immun. 57:3306-3313.
    • (1989) Infect. Immun. , vol.57 , pp. 3306-3313
    • Lee, S.F.1    Progulske-Fox, A.2    Erdos, G.W.3    Piacentini, D.A.4    Ayakawa, G.Y.5    Crowley, P.J.6    Bleiweis, A.S.7
  • 44
    • 0033819140 scopus 로고    scopus 로고
    • Programmed death in bacteria
    • Lewis, K. 2000. Programmed death in bacteria. Microbiol. Mol. Biol Rev. 64:503-514.
    • (2000) Microbiol. Mol. Biol Rev. , vol.64 , pp. 503-514
    • Lewis, K.1
  • 45
    • 0036233112 scopus 로고    scopus 로고
    • A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation
    • Li, Y. H., N. Tang, M. B. Aspiras, P. C. Lau, J. H. Lee, R. P. Ellen, and D. G. Cvitkovitch. 2002. A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation. J. Bacteriol. 184:2699-2708.
    • (2002) J. Bacteriol. , vol.184 , pp. 2699-2708
    • Li, Y.H.1    Tang, N.2    Aspiras, M.B.3    Lau, P.C.4    Lee, J.H.5    Ellen, R.P.6    Cvitkovitch, D.G.7
  • 46
    • 0023231033 scopus 로고
    • Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica A1
    • Lo, R. Y., C. A. Strathdee, and P. E. Shewen. 1987. Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica A1. Infect. Immun. 55:1987-1996.
    • (1987) Infect. Immun. , vol.55 , pp. 1987-1996
    • Lo, R.Y.1    Strathdee, C.A.2    Shewen, P.E.3
  • 47
    • 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
  • 48
    • 0028291159 scopus 로고
    • The gene of the N-acetyl-glucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis
    • Margot, P., C. Mauel, and D. Karamata. 1994. The gene of the N-acetyl-glucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis. Mol. Microbiol. 12:535-545.
    • (1994) Mol. Microbiol. , vol.12 , pp. 535-545
    • Margot, P.1    Mauel, C.2    Karamata, D.3
  • 49
    • 0034772911 scopus 로고    scopus 로고
    • Cloning of the Streptococcus mutans gene encoding glucan binding protein B and analysis of genetic diversity and protein production in clinical isolates
    • Mattos-Graner, R. O., S. Jin, W. F. King, T. Chen, D. J. Smith, and M. J. Duncan. 2001. Cloning of the Streptococcus mutans gene encoding glucan binding protein B and analysis of genetic diversity and protein production in clinical isolates. Infect. Immun. 69:6931-6941.
    • (2001) Infect. Immun. , vol.69 , pp. 6931-6941
    • Mattos-Graner, R.O.1    Jin, S.2    King, W.F.3    Chen, T.4    Smith, D.J.5    Duncan, M.J.6
  • 50
    • 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
  • 52
    • 0028275633 scopus 로고
    • Tripeptidase gene (pepT) of Lactococcus lactis: Molecular cloning and nucleotide sequencing of pepT and construction of a chromosomal deletion mutant
    • Mierau, I., A. J. Haandrikman, O. Velterop, P. S. Tan, K. L. Leenhouts, W. N. Konings, G. Venema, and J. Kok. 1994. Tripeptidase gene (pepT) of Lactococcus lactis: molecular cloning and nucleotide sequencing of pepT and construction of a chromosomal deletion mutant. J. Bacteriol. 176:2854-2861.
    • (1994) J. Bacteriol. , vol.176 , pp. 2854-2861
    • Mierau, I.1    Haandrikman, A.J.2    Velterop, O.3    Tan, P.S.4    Leenhouts, K.L.5    Konings, W.N.6    Venema, G.7    Kok, J.8
  • 53
    • 0028908856 scopus 로고
    • A Staphylococcus aureus autolysin that has an N-acetyl-muramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: Cloning, sequence analysis, and characterization
    • Oshida, T., M. Sugai, H. Komatsuzawa, Y. M. Hong, H. Suginaka, and A. Tomasz. 1995. A Staphylococcus aureus autolysin that has an N-acetyl-muramoyl-L- alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc. Natl. Acad. Sci. USA 92:285-289.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 285-289
    • Oshida, T.1    Sugai, M.2    Komatsuzawa, H.3    Hong, Y.M.4    Suginaka, H.5    Tomasz, A.6
  • 55
    • 0014836066 scopus 로고
    • Relationship between the location of autolysin, cell wall synthesis, and the development of resistance to cellular autolysis in Streptococcus faecalis after inhibition of protein synthesis
    • Pooley, H. M., and G. D. Shockman. 1970. Relationship between the location of autolysin, cell wall synthesis, and the development of resistance to cellular autolysis in Streptococcus faecalis after inhibition of protein synthesis. J. Bacteriol. 103:457-466.
    • (1970) J. Bacteriol. , vol.103 , pp. 457-466
    • Pooley, H.M.1    Shockman, G.D.2
  • 56
    • 0015251850 scopus 로고
    • Some properties of two autolytic-defective mutants of Streptococcus faecalis ATCC 9790
    • Pooley, H. M., G. D. Shockman, M. L. Higgins, and J. Porres-Juan. 1972. Some properties of two autolytic-defective mutants of Streptococcus faecalis ATCC 9790. J. Bacteriol. 109:423-431.
    • (1972) J. Bacteriol. , vol.109 , pp. 423-431
    • Pooley, H.M.1    Shockman, G.D.2    Higgins, M.L.3    Porres-Juan, J.4
  • 58
    • 3342944909 scopus 로고    scopus 로고
    • Inactivation of the ciaH Gene in Streptococcus mutans diminishes mutacin production and competence development, alters sucrose-dependent biofilm formation, and reduces stress tolerance
    • Qi, F., J. Merritt, R. Lux, and W. Shi. 2004. Inactivation of the ciaH Gene in Streptococcus mutans diminishes mutacin production and competence development, alters sucrose-dependent biofilm formation, and reduces stress tolerance. Infect. Immun. 72:4895-4899.
    • (2004) Infect. Immun. , vol.72 , pp. 4895-4899
    • Qi, F.1    Merritt, J.2    Lux, R.3    Shi, W.4
  • 59
    • 0028805257 scopus 로고
    • Glucosaminidase of Bacillus subtilis: Cloning, regulation, primary structure and biochemical characterization
    • Rashid, M. H., M. Mon, and J. Sekiguchi. 1995. Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization. Microbiology 141:2391-2404.
    • (1995) Microbiology , vol.141 , pp. 2391-2404
    • Rashid, M.H.1    Mon, M.2    Sekiguchi, J.3
  • 60
    • 0035143577 scopus 로고    scopus 로고
    • Identification and molecular analysis of PcsB, a protein required for cell wall separation of group B streptococcus
    • Reinscheid, D. J., B. Gottschalk, A. Schubert, B. J. Eikmanns, and G. S. Chhatwal. 2001. Identification and molecular analysis of PcsB, a protein required for cell wall separation of group B streptococcus. J. Bacteriol. 183:1175-1183.
    • (2001) J. Bacteriol. , vol.183 , pp. 1175-1183
    • Reinscheid, D.J.1    Gottschalk, B.2    Schubert, A.3    Eikmanns, B.J.4    Chhatwal, G.S.5
  • 61
    • 2342546598 scopus 로고    scopus 로고
    • Transcription of the Staphylococcus aureus cid and lrg murein hydrolase regulators is affected by sigma factor B
    • Rice, K. C., T. Patton, S. J. Yang, A. Dumoulin, M. Bischoff, and K. W. Bayles. 2004. Transcription of the Staphylococcus aureus cid and lrg murein hydrolase regulators is affected by sigma factor B. J. Bacteriol. 186:3029-3037.
    • (2004) J. Bacteriol. , vol.186 , pp. 3029-3037
    • Rice, K.C.1    Patton, T.2    Yang, S.J.3    Dumoulin, A.4    Bischoff, M.5    Bayles, K.W.6
  • 62
    • 0028983022 scopus 로고
    • Beta-lactam-induced bacteriolysis of amino acid-deprived Escherichia coli is dependent on phospholipid synthesis
    • Rodionov, D. G., A. G. Pisabarro, M. A. de Pedro, W. Kusser, and E. E. Ishiguro. 1995. Beta-lactam-induced bacteriolysis of amino acid-deprived Escherichia coli is dependent on phospholipid synthesis. J. Bacteriol. 177: 992-997.
    • (1995) J. Bacteriol. , vol.177 , pp. 992-997
    • Rodionov, D.G.1    Pisabarro, A.G.2    De Pedro, M.A.3    Kusser, W.4    Ishiguro, E.E.5
  • 63
    • 32244442842 scopus 로고    scopus 로고
    • LuxS impacts on LytA-dependent autolysis and on competence in Streptococcus pneumoniae
    • Romao, S., G. Memmi, M. R. Oggioni, and M. C. Trombe. 2006. LuxS impacts on LytA-dependent autolysis and on competence in Streptococcus pneumoniae. Microbiology 152:333-341.
    • (2006) Microbiology , vol.152 , pp. 333-341
    • Romao, S.1    Memmi, G.2    Oggioni, M.R.3    Trombe, M.C.4
  • 64
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: An organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch, J. W., and M. G. Caparon. 2005. The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol. Microbiol. 58:959-968.
    • (2005) Mol. Microbiol. , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 66
    • 0025288833 scopus 로고
    • Cloning and expression of gene fragments encoding the choline-binding domain of pneumococcal murein hydrolases
    • Sanchez-Puelles, J. M., J. M. Sanz, J. L. Garcia, and E. Garcia. 1990. Cloning and expression of gene fragments encoding the choline-binding domain of pneumococcal murein hydrolases. Gene 89:69-75.
    • (1990) Gene , vol.89 , pp. 69-75
    • Sanchez-Puelles, J.M.1    Sanz, J.M.2    Garcia, J.L.3    Garcia, E.4
  • 68
    • 0016415604 scopus 로고
    • Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria
    • Shaw, W. V. 1975. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol. 43:737-755.
    • (1975) Methods Enzymol. , vol.43 , pp. 737-755
    • Shaw, W.V.1
  • 69
    • 19744378673 scopus 로고    scopus 로고
    • Identification and characterization of an autolysin-encoding gene of Streptococcus mutans
    • Shibata, Y., M. Kawada, Y. Nakano, K. Toyoshima, and Y. Yamashita. 2005. Identification and characterization of an autolysin-encoding gene of Streptococcus mutans. Infect. Immun. 73:3512-3520.
    • (2005) Infect. Immun. , vol.73 , pp. 3512-3520
    • Shibata, Y.1    Kawada, M.2    Nakano, Y.3    Toyoshima, K.4    Yamashita, Y.5
  • 70
    • 0020653625 scopus 로고
    • Structure, function, and assembly of cell walls of gram-positive bacteria
    • Shockman, G. D., and J. F. Barrett. 1983. Structure, function, and assembly of cell walls of gram-positive bacteria. Annu. Rev. Microbiol. 37:501-527.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 501-527
    • Shockman, G.D.1    Barrett, J.F.2
  • 72
    • 0014072430 scopus 로고
    • The autolytic enzyme system of Streptococcus faecalis. II. Partial characterization of the autolysin and its substrate
    • Shockman, G. D., J. S. Thompson, and M. J. Conover. 1967. The autolytic enzyme system of Streptococcus faecalis. II. Partial characterization of the autolysin and its substrate. Biochemistry 6:1054-1065.
    • (1967) Biochemistry , vol.6 , pp. 1054-1065
    • Shockman, G.D.1    Thompson, J.S.2    Conover, M.J.3
  • 73
    • 0018367629 scopus 로고
    • Morphological and physiological study of autolytic-defective Streptococcus faecium strains
    • Shungu, D. L., J. B. Cornett, and G. D. Shockman. 1979. Morphological and physiological study of autolytic-defective Streptococcus faecium strains. J. Bacteriol. 138:598-608.
    • (1979) J. Bacteriol. , vol.138 , pp. 598-608
    • Shungu, D.L.1    Cornett, J.B.2    Shockman, G.D.3
  • 74
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith, T. J., S. A. Blackman, and S. J. Foster. 2000. Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146:249-262.
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 76
    • 0024552790 scopus 로고
    • Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella haemolytica leukotoxin determinant
    • Strathdee, C. A., and R. Y. Lo. 1989. Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella haemolytica leukotoxin determinant. J. Bacteriol. 171:916-928.
    • (1989) J. Bacteriol. , vol.171 , pp. 916-928
    • Strathdee, C.A.1    Lo, R.Y.2
  • 77
    • 0028986933 scopus 로고
    • Identification of endo-beta-N-acetyl-glucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus
    • Sugai, M., H. Koraatsuzawa, T. Akiyama, Y. M. Hong, T. Oshida, Y. Miyake, T. Yamaguchi, and H. Suginaka. 1995. Identification of endo-beta-N-acetyl- glucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus. J. Bacteriol. 177:1491-1496.
    • (1995) J. Bacteriol. , vol.177 , pp. 1491-1496
    • Sugai, M.1    Koraatsuzawa, H.2    Akiyama, T.3    Hong, Y.M.4    Oshida, T.5    Miyake, Y.6    Yamaguchi, T.7    Suginaka, H.8
  • 79
    • 0015578690 scopus 로고
    • Autolysis of Listeria monocytogenes
    • Tyrrell, E. A. 1973. Autolysis of Listeria monocytogenes. J. Bacteriol. 113: 1046-1048.
    • (1973) J. Bacteriol. , vol.113 , pp. 1046-1048
    • Tyrrell, E.A.1
  • 81
    • 0035125913 scopus 로고    scopus 로고
    • Construction of a new integration vector for use in Streptococcus mutans
    • Wen, Z. T., and R. A. Burne. 2001. Construction of a new integration vector for use in Streptococcus mutans. Plasmid 45:31-36.
    • (2001) Plasmid , vol.45 , pp. 31-36
    • Wen, Z.T.1    Burne, R.A.2
  • 82
    • 1942507978 scopus 로고    scopus 로고
    • LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation
    • Wen, Z. T., and R. A. Burne. 2004. LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation. J. Bacteriol. 186:2682-2691.
    • (2004) J. Bacteriol. , vol.186 , pp. 2682-2691
    • Wen, Z.T.1    Burne, R.A.2
  • 83
    • 0032803541 scopus 로고    scopus 로고
    • The autolysin-encoding gene (lytA) of Streptococcus pneumoniae displays restricted allelic variation despite localized recombination events with genes of pneumococcal bacteriophage encoding cell wall lytic enzymes
    • Whatmore, A. M., and C. G. Dowson. 1999. The autolysin-encoding gene (lytA) of Streptococcus pneumoniae displays restricted allelic variation despite localized recombination events with genes of pneumococcal bacteriophage encoding cell wall lytic enzymes. Infect. Immun. 67:4551-4556.
    • (1999) Infect. Immun. , vol.67 , pp. 4551-4556
    • Whatmore, A.M.1    Dowson, C.G.2
  • 84
    • 0141593638 scopus 로고    scopus 로고
    • Effect of acidic pH on expression of surface-associated proteins of Streptococcus oralis
    • Wilkins, J. C., D. Beighton, and K. A. Homer. 2003. Effect of acidic pH on expression of surface-associated proteins of Streptococcus oralis. Appl. Environ. Microbiol. 69:5290-5296.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5290-5296
    • Wilkins, J.C.1    Beighton, D.2    Homer, K.A.3
  • 85
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren, B. W. 1991. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol. Microbiol. 5:797-803.
    • (1991) Mol. Microbiol. , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 86
    • 0027191827 scopus 로고
    • The lap gene of Listeria monocytogenes is essential for cell viability, and its gene product, p60, has bacteriolytic activity
    • Wuenscher, M. D., S. Kohler, A. Bubert, U. Gerike, and W. Goebel. 1993. The lap gene of Listeria monocytogenes is essential for cell viability, and its gene product, p60, has bacteriolytic activity. J. Bacteriol. 175:3491-3501.
    • (1993) J. Bacteriol. , vol.175 , pp. 3491-3501
    • Wuenscher, M.D.1    Kohler, S.2    Bubert, A.3    Gerike, U.4    Goebel, W.5
  • 88
    • 24344450017 scopus 로고    scopus 로고
    • A LysR-type regulator, CidR, is required for induction of the Staphylococcus aureus cidABC operon
    • Yang, S. J., K. C. Rice, R. J. Brown, T. G. Fatten, L. E. Liou, Y. H. Park, and K. W. Bayles. 2005. A LysR-type regulator, CidR, is required for induction of the Staphylococcus aureus cidABC operon. J. Bacteriol. 187:5893-5900.
    • (2005) J. Bacteriol. , vol.187 , pp. 5893-5900
    • Yang, S.J.1    Rice, K.C.2    Brown, R.J.3    Fatten, T.G.4    Liou, L.E.5    Park, Y.H.6    Bayles, K.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.