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Volumn 68, Issue 11, 2002, Pages 5549-5553

Isolation and molecular analysis of the gene cluster for the arginine deiminase system from Streptococcus gordonii DL1

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; BIOFILMS; ECOLOGY; ENZYMES; GENES; GLUCOSE; NUCLEIC ACID SEQUENCES; PH EFFECTS;

EID: 0036840306     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.68.11.5549-5553.2002     Document Type: Article
Times cited : (75)

References (37)
  • 1
    • 0001428082 scopus 로고
    • Determination of citrulline and allantoin and demonstration of citrulline in blood plasma
    • Archibald, R. M. 1944. Determination of citrulline and allantoin and demonstration of citrulline in blood plasma. J. Biol. Chem. 156:121-142.
    • (1944) J. Biol. Chem. , vol.156 , pp. 121-142
    • Archibald, R.M.1
  • 3
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322
    • Bartolome, B., Y. Jubete, E. Martinez, and F. dela Cruz, 1991. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322. Gene 102:75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolome, B.1    Jubete, Y.2    Martinez, E.3    Dela Cruz, F.4
  • 4
    • 0024584223 scopus 로고
    • Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of Pseudomonas aeruginosa
    • Baur, H., E. Luethi, V. Stalon, A. Mercenier, and D. Haas. 1989. Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of Pseudomonas aeruginosa. Eur. J. Biochem. 179:53-60.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 53-60
    • Baur, H.1    Luethi, E.2    Stalon, V.3    Mercenier, A.4    Haas, D.5
  • 5
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 6
    • 0023414270 scopus 로고
    • Environmental pH as a factor in the competition between strains of the oral streptococci Streptococcus mutans. S. sanguis, and "S. mitior" growing in continuous culture
    • Bowden, G. H., and I. R. Hamilton. 1987. Environmental pH as a factor in the competition between strains of the oral streptococci Streptococcus mutans. S. sanguis, and "S. mitior" growing in continuous culture. Can. J. Microbiol. 33:824-827.
    • (1987) Can. J. Microbiol. , vol.33 , pp. 824-827
    • Bowden, G.H.1    Hamilton, I.R.2
  • 7
    • 0027956735 scopus 로고
    • Mutant Escherichia coli arginine repressor proteins that fail to bind L-arginine, yet retain the ability to bind their normal DNA-binding sites
    • Burke, M., A. F. Merican, and D. J. Sherratt. 1994. Mutant Escherichia coli arginine repressor proteins that fail to bind L-arginine, yet retain the ability to bind their normal DNA-binding sites. Mol. Microbiol. 13:609-618.
    • (1994) Mol. Microbiol. , vol.13 , pp. 609-618
    • Burke, M.1    Merican, A.F.2    Sherratt, D.J.3
  • 8
    • 0034560281 scopus 로고    scopus 로고
    • Alkali production by oral bacteria and protection against dental caries
    • Burne, R. A., and R. E. Marquis. 2000. Alkali production by oral bacteria and protection against dental caries. FEMS Microbiol. Lett. 193:1-6.
    • (2000) FEMS Microbiol. Lett. , vol.193 , pp. 1-6
    • Burne, R.A.1    Marquis, R.E.2
  • 9
    • 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. M. 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.M.3    Penders, J.E.4
  • 10
    • 0023946229 scopus 로고
    • Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance
    • Casiano-Colon, A., and R. E. Marquis. 1988. Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance. Appl. Environ. Microbiol. 54:1318-1324.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1318-1324
    • Casiano-Colon, A.1    Marquis, R.E.2
  • 12
    • 0030029962 scopus 로고    scopus 로고
    • Analysis of Streptococcus salivarius urease expression using continuous chemostat culture
    • Chen, Y. M., and R. A. Burne. 1996. Analysis of Streptococcus salivarius urease expression using continuous chemostat culture. FEMS Microbiol. Lett. 135:223-229.
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 223-229
    • Chen, Y.M.1    Burne, R.A.2
  • 13
    • 0031768170 scopus 로고    scopus 로고
    • Transcriptional regulation of the Streptococcus salivarius 57.I urease operon
    • Chen, Y. M., C. A. Weaver, D. R. Mendelsohn, and R. A. Burne. 1998. Transcriptional regulation of the Streptococcus salivarius 57.I urease operon. J. Bacteriol. 180:5769-5775.
    • (1998) J. Bacteriol. , vol.180 , pp. 5769-5775
    • Chen, Y.M.1    Weaver, C.A.2    Mendelsohn, D.R.3    Burne, R.A.4
  • 14
    • 0034059267 scopus 로고    scopus 로고
    • Characterization of recombinant, ureolytic Streptococcus mutans demonstrates an inverse relationship between dental plaque ureolytic capacity and cariogenicity
    • Clancy, K. A., S. Pearson, W. H. Bowen, and R. A. Burne. 2000. Characterization of recombinant, ureolytic Streptococcus mutans demonstrates an inverse relationship between dental plaque ureolytic capacity and cariogenicity. Infect. Immun. 68:2621-2629.
    • (2000) Infect. Immun. , vol.68 , pp. 2621-2629
    • Clancy, K.A.1    Pearson, S.2    Bowen, W.H.3    Burne, R.A.4
  • 15
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane α-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., E. Wallin, I. Simon, G. von Heijne, and A. Elofsson. 1997. Prediction of transmembrane α-helices in prokaryotic membrane proteins: The dense alignment surface method. Protein Eng. 10:673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 16
  • 17
    • 0032463639 scopus 로고    scopus 로고
    • Turning on and turning off the arginine deiminase system in oral streptococci
    • Curran, T. M., Y. Ma, G. C. Rutherford, and R. E. Marquis. 1998. Turning on and turning off the arginine deiminase system in oral streptococci. Can. J. Microbiol. 44:1078-1085.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 1078-1085
    • Curran, T.M.1    Ma, Y.2    Rutherford, G.C.3    Marquis, R.E.4
  • 18
    • 0030725163 scopus 로고    scopus 로고
    • The arginine deiminase pathway in Rhizobium etli: DNA sequence analysis and functional study of the arcABC genes
    • D'Hooghe, I., C. Vander Wauven, J. Michiels, C. Tricot, P. de Wilde, J. Vanderleyden, and V. Stalon. 1997. The arginine deiminase pathway in Rhizobium etli: DNA sequence analysis and functional study of the arcABC genes. J. Bacteriol. 179:7403-7409.
    • (1997) J. Bacteriol. , vol.179 , pp. 7403-7409
    • D'Hooghe, I.1    Vander Wauven, C.2    Michiels, J.3    Tricot, C.4    De Wilde, P.5    Vanderleyden, J.6    Stalon, V.7
  • 19
    • 0021037967 scopus 로고
    • Coordinately repressible arginine deiminase system in Streptococcus sanguis
    • Ferro, K. J., G. R. Bender, and R. E. Marquis. 1983. Coordinately repressible arginine deiminase system in Streptococcus sanguis. Curr. Microbiol. 9:145-150.
    • (1983) Curr. Microbiol. , vol.9 , pp. 145-150
    • Ferro, K.J.1    Bender, G.R.2    Marquis, R.E.3
  • 21
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28:351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 22
    • 0001823786 scopus 로고
    • Recombinant PCR
    • M. A. Innis, D. H. Gelfand, and J. J. White (ed.). Academic Press, Inc., San Francisco, Calif.
    • Higuchi, R. 1990. Recombinant PCR, p. 177-183. In M. A. Innis, D. H. Gelfand, and J. J. White (ed.), PCR Protocols: A Guide to Methods and Applications. Academic Press, Inc., San Francisco, Calif.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 23
    • 0021274224 scopus 로고
    • Protein differentiation: A comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12
    • Houghton, J. E., D. A. Bencini, G. A. O'Donovan, and J. R. Wild. 1984. Protein differentiation: A comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 81:4864-4868.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4864-4868
    • Houghton, J.E.1    Bencini, D.A.2    O'Donovan, G.A.3    Wild, J.R.4
  • 24
    • 0017202855 scopus 로고
    • Transformation of Streptococcus sanguis strain Challis by plasmid DNA from Streptococcusfaecalis
    • LeBlanc, D. J., and F. P. Hassell. 1976. Transformation of Streptococcus sanguis strain Challis by plasmid DNA from Streptococcusfaecalis. J. Bacteriol. 128:347-355.
    • (1976) J. Bacteriol. , vol.128 , pp. 347-355
    • LeBlanc, D.J.1    Hassell, F.P.2
  • 25
    • 0020287153 scopus 로고
    • Characterization of two tetracycline resistance determinants in Streptococcus faecalis
    • LeBlanc, D. J., and L. N. Lee. 1982. Characterization of two tetracycline resistance determinants in Streptococcus faecalis. JH1. J. Bacteriol. 150:835-843.
    • (1982) JH1. J. Bacteriol. , vol.150 , pp. 835-843
    • LeBlanc, D.J.1    Lee, L.N.2
  • 26
    • 0032906547 scopus 로고    scopus 로고
    • The ArgR regulatory protein, a helper to the anaerobic regulator ANR during transcriptional activation of the arcD promoter in Pseudomonas aeruginosa
    • Lu, C. D., H. Winteler, A. Abdelal, and D. Haas. 1999. The ArgR regulatory protein, a helper to the anaerobic regulator ANR during transcriptional activation of the arcD promoter in Pseudomonas aeruginosa. J. Bacteriol. 181:2459-2464.
    • (1999) J. Bacteriol. , vol.181 , pp. 2459-2464
    • Lu, C.D.1    Winteler, H.2    Abdelal, A.3    Haas, D.4
  • 27
    • 0032440064 scopus 로고    scopus 로고
    • The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor ArgR
    • Maghnouj, A., T. F. de Sousa Cabral, V. Stalon, and C. Vander Wauven. 1998. The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor ArgR. J. Bacteriol. 180:6468-6475.
    • (1998) J. Bacteriol. , vol.180 , pp. 6468-6475
    • Maghnouj, A.1    De Sousa Cabral, T.F.2    Stalon, V.3    Vander Wauven, C.4
  • 28
    • 0032054533 scopus 로고    scopus 로고
    • Carbamate kinase from Enterococcus faecalis and Enterococcus faecium: Cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase
    • Marina, A., M. Uriarte, B. Barcelona, V. Fresquet, J. Cervera, and V. Rubio. 1998. Carbamate kinase from Enterococcus faecalis and Enterococcus faecium: Cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase. Eur. J. Biochem. 253:280-291.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 280-291
    • Marina, A.1    Uriarte, M.2    Barcelona, B.3    Fresquet, V.4    Cervera, J.5    Rubio, V.6
  • 29
    • 0023120802 scopus 로고
    • Arginine deiminase system and bacterial adaptation to acid environments
    • Marquis, R. E., G. R. Bender, D. R. Murray, and A. Wong. 1987. Arginine deiminase system and bacterial adaptation to acid environments. Appl. Environ. Microbiol. 53:198-200.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 198-200
    • Marquis, R.E.1    Bender, G.R.2    Murray, D.R.3    Wong, A.4
  • 30
    • 0025865798 scopus 로고
    • Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems
    • Perez-Casal, J., M. G. Caparon, and J. R. Scott. 1991. Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems J. Bacteriol. 173:2617-2624.
    • (1991) J. Bacteriol. , vol.173 , pp. 2617-2624
    • Perez-Casal, J.1    Caparon, M.G.2    Scott, J.R.3
  • 31
    • 0000487088 scopus 로고
    • Changes in hydrogen-ion concentration on tooth surfaces and in carious lesions
    • Stephan, R. M. 1940. Changes in hydrogen-ion concentration on tooth surfaces and in carious lesions. J. Am. Dent. 27:718-723.
    • (1940) J. Am. Dent. , vol.27 , pp. 718-723
    • Stephan, R.M.1
  • 32
    • 0032531265 scopus 로고    scopus 로고
    • Dissecting the molecular details of prokaryotic transcriptional control by surface plasmon resonance: The methionine and arginine repressor proteins
    • Stockley, P. G., A. J. Baron, C. M. Wild, I. D. Parsons, C. M. Miller, C. A. Holtham, and S. Baumberg. 1998. Dissecting the molecular details of prokaryotic transcriptional control by surface plasmon resonance: The methionine and arginine repressor proteins. Biosens. Bioelectron. 13:637-650.
    • (1998) Biosens. Bioelectron. , vol.13 , pp. 637-650
    • Stockley, P.G.1    Baron, A.J.2    Wild, C.M.3    Parsons, I.D.4    Miller, C.M.5    Holtham, C.A.6    Baumberg, S.7
  • 33
    • 0033118267 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria
    • Stülke, J., and W. Hillen. 1999. Carbon catabolite repression in bacteria. Curr. Opin. Microbiol. 2:195-201.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 195-201
    • Stülke, J.1    Hillen, W.2
  • 34
    • 0028129470 scopus 로고
    • Mutational analysis of the arginine repressor of Escherichia coli
    • Tian, G., and W. K. Maas. 1994. Mutational analysis of the arginine repressor of Escherichia coli. Mol. Microbiol. 13:599-608.
    • (1994) Mol. Microbiol. , vol.13 , pp. 599-608
    • Tian, G.1    Maas, W.K.2
  • 35
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    • Van Duyne, G. D., G. Ghosh, W. K. Maas, and P. B. Sigler. 1996. Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J. Mol. Biol. 256:377-391.
    • (1996) J. Mol. Biol. , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 37
    • 0031856844 scopus 로고    scopus 로고
    • Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sake
    • Zúñiga, M., M. Champomier-Verges, M. Zagorec, and G. Pérez-Martínez. 1998. Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sake. J. Bacteriol. 180:4154-4159.
    • (1998) J. Bacteriol. , vol.180 , pp. 4154-4159
    • Zúñiga, M.1    Champomier-Verges, M.2    Zagorec, M.3    Pérez-Martínez, G.4


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