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Volumn 86, Issue 1, 2003, Pages 96-104

Detection and localization of a peptidoglycan hydrolase in Lactobacillus delbrueckii subsp. bulgaricus

Author keywords

Electron and fluorescence microscopy; Lactobacillus; Peptidoglycan hydrolase

Indexed keywords

BACTERIA (MICROORGANISMS); ENTEROCOCCUS; ENTEROCOCCUS HIRAE; LACTOBACILLUS; LACTOBACILLUS DELBRUECKII; LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS; MICROCOCCUS; MICROCOCCUS LUTEUS;

EID: 0038320880     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(03)73588-7     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 0000918763 scopus 로고
    • Influence of pH, lactose and lactic acid on the growth of Streptococcus cremoris: A kinetic study
    • Bibal, B., G. Goma, Y. Vayssier, and A. Pareilleux. 1988. Influence of pH, lactose and lactic acid on the growth of Streptococcus cremoris: A kinetic study. Appl. Microbiol. Biotechnol. 28:340-344.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 340-344
    • Bibal, B.1    Goma, G.2    Vayssier, Y.3    Pareilleux, A.4
  • 4
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G., J. Kok, K. J. Leenhouts, M. Dabrowska, G. Venema, and A. J. Haandrikman. 1995. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 177:1554-1563.
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 5
    • 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
  • 7
    • 0033678872 scopus 로고    scopus 로고
    • Autolysis of dairy leuconostocs and detection of peptidoglycan hydrolases by renaturing SDS-PAGE
    • Cibik, R., and M.-P. Chapot-Chartier. 2000. Autolysis of dairy leuconostocs and detection of peptidoglycan hydrolases by renaturing SDS-PAGE. J. Appl. Microbiol. 89:862-869.
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 862-869
    • Cibik, R.1    Chapot-Chartier, M.-P.2
  • 8
    • 0035140786 scopus 로고    scopus 로고
    • Identification of Mur, an atypical peptidoglycan hydrolase derived from Leuconostoc citreum
    • Cibik, R., P. Tailliez, P. Langella, and M.-P. Chapot-Chartier. 2001. Identification of Mur, an atypical peptidoglycan hydrolase derived from Leuconostoc citreum. Appl. Environ. Microbiol. 67:858-864.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 858-864
    • Cibik, R.1    Tailliez, P.2    Langella, P.3    Chapot-Chartier, M.-P.4
  • 9
    • 0039798057 scopus 로고
    • Accelerated ripening of ras cheese with a commercial proteinase and intracellular enzymes from Lactobacillus delbrueckii ssp. bulgaricus, Propionibacterium freudenreichii and Brevibacterium linens
    • Ezzat, N. 1990. Accelerated ripening of ras cheese with a commercial proteinase and intracellular enzymes from Lactobacillus delbrueckii ssp. bulgaricus, Propionibacterium freudenreichii and Brevibacterium linens. Lait. 70:459-466.
    • (1990) Lait. , vol.70 , pp. 459-466
    • Ezzat, N.1
  • 10
    • 0011988827 scopus 로고
    • Peptide hydrolases from thermobacterium group of lactobacilli III. Characterization of intracellular peptidases
    • Ezzat, N., M. el Soda, M. J. Desmazeaud, and A. Ismail. 1986. Peptide hydrolases from thermobacterium group of lactobacilli III. Characterization of intracellular peptidases. Lait. 66:445-451.
    • (1986) Lait. , vol.66 , pp. 445-451
    • Ezzat, N.1    El Soda, M.2    Desmazeaud, M.J.3    Ismail, A.4
  • 11
    • 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
  • 14
    • 0034213799 scopus 로고    scopus 로고
    • Mur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain
    • Husson-Kao, C., J. Mengaud, L. Benbadis, and M.-P. Chapot-Chartier. 2000. Mur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain. FEMS Microbiol. Lett. 187:69-76.
    • (2000) FEMS Microbiol. Lett. , vol.187 , pp. 69-76
    • Husson-Kao, C.1    Mengaud, J.2    Benbadis, L.3    Chapot-Chartier, M.-P.4
  • 16
    • 0040687323 scopus 로고    scopus 로고
    • Some factors influencing the autolysis of Lactobacillus bulgaricus and Lactobacillus casei
    • Kang, O. J., L. P. Vézina, S. Laberge, and R. E. Simard. 1998a. Some factors influencing the autolysis of Lactobacillus bulgaricus and Lactobacillus casei. J. Dairy Sci. 81:639-646.
    • (1998) J. Dairy Sci. , vol.81 , pp. 639-646
    • Kang, O.J.1    Vézina, L.P.2    Laberge, S.3    Simard, R.E.4
  • 17
    • 4043082429 scopus 로고    scopus 로고
    • Mechanism of autolysis of isolated cell walls of Lactobacillus delbrueckii ssp. bulgaricus
    • Kang, O. J., L. P. Vézina, S. Laberge, and R. E. Simard. 1998b. Mechanism of autolysis of isolated cell walls of Lactobacillus delbrueckii ssp. bulgaricus. Microbiol. Nutri. Aliments. 16:17-24.
    • (1998) Microbiol. Nutri. Aliments. , vol.16 , pp. 17-24
    • Kang, O.J.1    Vézina, L.P.2    Laberge, S.3    Simard, R.E.4
  • 18
    • 0026691017 scopus 로고
    • Extracellular and cellular distribution of muramidase-2 and muramidase-1 of E. hirae ATCC 9790
    • Kariyama, R., and G. D. Shockman. 1992. Extracellular and cellular distribution of muramidase-2 and muramidase-1 of E. hirae ATCC 9790. J. Bacteriol. 174:3236-3241.
    • (1992) J. Bacteriol. , vol.174 , pp. 3236-3241
    • Kariyama, R.1    Shockman, G.D.2
  • 20
    • 0030133706 scopus 로고    scopus 로고
    • Detection and localization of peptidases in Lactococcus lactis with monoclonal antibodies
    • Laan, H., R. E. Haverkort, L. de Leij, and W. N. Konings. 1996. Detection and localization of peptidases in Lactococcus lactis with monoclonal antibodies. J. Dairy Res. 63:245-256.
    • (1996) J. Dairy Res. , vol.63 , pp. 245-256
    • Laan, H.1    Haverkort, R.E.2    De Leij, L.3    Konings, W.N.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1974. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1974) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0000569788 scopus 로고
    • Influence de plusieurs facteurs sur l'autolyse de L. helveticus CNRZ 414
    • Lortal, S., P. Boyaval, and J. Van Heijenoort. 1989. Influence de plusieurs facteurs sur l'autolyse de L. helveticus CNRZ 414. Lait. 69:223-231.
    • (1989) Lait. , vol.69 , pp. 223-231
    • Lortal, S.1    Boyaval, P.2    Van Heijenoort, J.3
  • 23
    • 0030853794 scopus 로고    scopus 로고
    • Electrophoretic pattern of peptidoglycan hydrolases, a new tool for bacterial species identification: Application to 10 Lactobacillus species
    • Lortal, S., F. Valence, C. Bizet, and J. L. Maubois. 1997. Electrophoretic pattern of peptidoglycan hydrolases, a new tool for bacterial species identification: Application to 10 Lactobacillus species. Res. Microbiol. 148:461-474.
    • (1997) Res. Microbiol. , vol.148 , pp. 461-474
    • Lortal, S.1    Valence, F.2    Bizet, C.3    Maubois, J.L.4
  • 24
    • 0028269929 scopus 로고
    • Purification and characterization of mature, membrane-associ-ated cell envelope proteinase of Lactobacillus helveticus L89
    • Martin-Hernandez, M. C., A. C. Alting, and F. A. Exterkate. 1993. Purification and characterization of mature, membrane-associ-ated cell envelope proteinase of Lactobacillus helveticus L89. Appl. Microbiol. Biotechnol. 40:828-834.
    • (1993) Appl. Microbiol. Biotechnol. , vol.40 , pp. 828-834
    • Martin-Hernandez, M.C.1    Alting, A.C.2    Exterkate, F.A.3
  • 25
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre, W. W., and O. Schneewind. 1999. Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol. Mol. Biol. Rev. 63:174-229.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 26
    • 0002449645 scopus 로고
    • Role of tissue processing in colloidal gold methods
    • Chap. 3. M. A. Hayat, ed. Academic Press Inc., California
    • Newman, G. R., and J. A. Hobot. 1989. Role of tissue processing in colloidal gold methods. Chap. 3 in Colloidal Gold, Principale Methods and Applications (vol. 2). M. A. Hayat, ed. Academic Press Inc., California.
    • (1989) Colloidal Gold, Principale Methods and Applications , vol.2
    • Newman, G.R.1    Hobot, J.A.2
  • 27
    • 0020429060 scopus 로고
    • The preservation of ultrastructure and antigenicity
    • Oxford
    • Newman, G. R., B. Jasani, and E. D. Williams. 1982. The preservation of ultrastructure and antigenicity. J. Microsc. (Oxford) 127. Rp5.
    • (1982) J. Microsc. , vol.127
    • Newman, G.R.1    Jasani, B.2    Williams, E.D.3
  • 28
    • 0014240645 scopus 로고
    • The Nomarski interference-contrast microscope. An experimental basis for image interpretation
    • Padawer, J. 1968. The Nomarski interference-contrast microscope. An experimental basis for image interpretation. J. Royal Microscopical Soc. 88:305-349.
    • (1968) J. Royal Microscopical Soc. , vol.88 , pp. 305-349
    • Padawer, J.1
  • 29
    • 0024101177 scopus 로고
    • Cloning, sequencing, and expression of a Bacillus bacteriolytic enzyme in Escherichia coli
    • Potvin, C., D. Leclerc, G. Tremblay, A. Asselin, and G. Bellemare. 1988. Cloning, sequencing, and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. Mol. Gen. Genet. 214:241-248.
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 241-248
    • Potvin, C.1    Leclerc, D.2    Tremblay, G.3    Asselin, A.4    Bellemare, G.5
  • 30
    • 0034058048 scopus 로고    scopus 로고
    • Simultaneous immunofluorescent detection of coentrapped cells in gel beads
    • Prioult, G., C. Lacroix, C. Turcotte, and F. Ismail. 2000. Simultaneous immunofluorescent detection of coentrapped cells in gel beads. Appl. Environ. Microbiol. 66:2216-2219.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2216-2219
    • Prioult, G.1    Lacroix, C.2    Turcotte, C.3    Ismail, F.4
  • 31
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electronopaque stain in electron microscopy
    • Reynolds, E. S. 1963. The use of lead citrate at high pH as an electronopaque stain in electron microscopy. J. Cell Biol. 117:208-212.
    • (1963) J. Cell Biol. , vol.117 , pp. 208-212
    • Reynolds, E.S.1
  • 32
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • J. M. Ghuysen and R. Hakenbeck, ed. Elsevier Science, London
    • Shockman, G. D., and J. V. Höltje. 1994. Microbial peptidoglycan (murein) hydrolases. Pages 131-166 in Bacterial Cell Wall. J. M. Ghuysen and R. Hakenbeck, ed. Elsevier Science, London.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.V.2
  • 33
    • 0001868959 scopus 로고
    • Gold markers for single and double immunolabelling of ultrathin cryosections
    • Polak Varndell eds., Elsevier Science, B. V.
    • Slot, J. W., and H. J. Geuze. 1984. Gold markers for single and double immunolabelling of ultrathin cryosections. Pages 129-142 in Immunolabelling for Electron Microscopy. Polak Varndell eds., Elsevier Science, B. V.
    • (1984) Immunolabelling for Electron Microscopy , pp. 129-142
    • Slot, J.W.1    Geuze, H.J.2
  • 34
    • 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
  • 35
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H. T., T. Staehelin, and J. Gallant. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehelin, T.2    Gallant, J.3
  • 36
    • 0029150758 scopus 로고
    • Zymogram and preliminary characterization of Lactobacillus helveticus autolysins
    • Valence, F., and S. Lortal. 1995. Zymogram and preliminary characterization of Lactobacillus helveticus autolysins. Appl. Environ. Microbiol. 61:3391-3399.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3391-3399
    • Valence, F.1    Lortal, S.2
  • 37
    • 0028121702 scopus 로고
    • Autolysis and proteolysis in different strains of starter bacteria during Cheddar cheese ripening
    • Wilkinson, M. G., T. P. Guinee, D. M. O'Callaghen, and P. F. Fox. 1994. Autolysis and proteolysis in different strains of starter bacteria during Cheddar cheese ripening. J. Dairy Res. 61:249-262.
    • (1994) J. Dairy Res. , vol.61 , pp. 249-262
    • Wilkinson, M.G.1    Guinee, T.P.2    O'Callaghen, D.M.3    Fox, P.F.4
  • 38
    • 0020634657 scopus 로고
    • An alternative fixation-processing method for preembedding ultra structural immunocytochemistry of cytoplasmic antigens: The GBS (glutaraldehyde-borohydride-saponin) procedure
    • Willingham, M. C. 1983. An alternative fixation-processing method for preembedding ultra structural immunocytochemistry of cytoplasmic antigens: The GBS (glutaraldehyde-borohydride-saponin) procedure. J. Histochem. Cytochem. 31:791-798.
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 791-798
    • Willingham, M.C.1
  • 39
    • 0027373433 scopus 로고
    • Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790
    • Yamamoto, N., A. Akino, and T. Takamo. 1993. Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790. J. Biochem. 114:740-745.
    • (1993) J. Biochem. , vol.114 , pp. 740-745
    • Yamamoto, N.1    Akino, A.2    Takamo, T.3


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