메뉴 건너뛰기




Volumn 65, Issue 2, 1999, Pages 569-577

Identification and characterization of a lysis module present in a large proportion of bacteriophages infecting Streptococcus thermophilus

Author keywords

[No Author keywords available]

Indexed keywords

ISOCITRATE DEHYDROGENASE;

EID: 0032976001     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.2.569-577.1999     Document Type: Article
Times cited : (45)

References (69)
  • 2
    • 0028357986 scopus 로고
    • Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins
    • Arendt, E. K., C. Daly, G. F. Fitzgerald, and M. van de Guchte. 1994. Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins. Appl. Environ. Microbiol. 60:1875-1883.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1875-1883
    • Arendt, E.K.1    Daly, C.2    Fitzgerald, G.F.3    Van De Guchte, M.4
  • 3
    • 0025641630 scopus 로고
    • Characterisation and comparison of virulent bacteriophages of Streptococcus thermophilus isolated from yogurt
    • Benbadis, L., M. Faelen, P. Slos, A. Fazel, and A. Mercenier. 1990. Characterisation and comparison of virulent bacteriophages of Streptococcus thermophilus isolated from yogurt. Biochimie 72:855-862.
    • (1990) Biochimie , vol.72 , pp. 855-862
    • Benbadis, L.1    Faelen, M.2    Slos, P.3    Fazel, A.4    Mercenier, A.5
  • 4
    • 0027981084 scopus 로고
    • Cloning, molecular characterization, and expression of the genes encoding the lytic functions of the lactococcal bacteriophage φLC3: A dual lysis system of modular design
    • Birkeland, N.-K. 1994. Cloning, molecular characterization, and expression of the genes encoding the lytic functions of the lactococcal bacteriophage φLC3: a dual lysis system of modular design. Can. J. Microbiol. 40:658-665.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 658-665
    • Birkeland, N.-K.1
  • 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
    • 0026542734 scopus 로고
    • Taxonomic characterisation of Leuconostoc mesenteroides and Leuconostoc oenos bacteriophages
    • Boizet, B., M. Mata, O. Mignot, P. Ritzenthaler, and T. Sozzi. 1992. Taxonomic characterisation of Leuconostoc mesenteroides and Leuconostoc oenos bacteriophages. FEMS Microbiol. Lett. 90:211-216.
    • (1992) FEMS Microbiol. Lett. , vol.90 , pp. 211-216
    • Boizet, B.1    Mata, M.2    Mignot, O.3    Ritzenthaler, P.4    Sozzi, T.5
  • 7
    • 0030860104 scopus 로고    scopus 로고
    • Molecular analysis of lytic genes of bacteriophage 80α of S. Aureus
    • Bon, J., N. Mani, and R. K. Jayaswal. 1997. Molecular analysis of lytic genes of bacteriophage 80α of S. aureus. Can. J. Microbiol. 43:612-616.
    • (1997) Can. J. Microbiol. , vol.43 , pp. 612-616
    • Bon, J.1    Mani, N.2    Jayaswal, R.K.3
  • 8
    • 0028864083 scopus 로고
    • Sequence analysis of the Lactococcus lactis temperate bacteriophage BK5-T and demonstration that the phage DNA has cohesive ends
    • Boyce, J. D., B. E. Davidson, and A. J. Hillier. 1995. Sequence analysis of the Lactococcus lactis temperate bacteriophage BK5-T and demonstration that the phage DNA has cohesive ends. Appl. Environ. Microbiol. 61:4089-4098.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4089-4098
    • Boyce, J.D.1    Davidson, B.E.2    Hillier, A.J.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.M.1
  • 10
    • 0028110412 scopus 로고
    • Detection and classification of Streptococcus thermophilus bacteriophages isolated from industrial milk fermentation
    • Brüssow, H., M. Frémont, A. Bruttin, J. Sidoti, A. Constable, and V. Fryder. 1994. Detection and classification of Streptococcus thermophilus bacteriophages isolated from industrial milk fermentation. Appl. Environ. Microbiol. 60:4537-4543.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4537-4543
    • Brüssow, H.1    Frémont, M.2    Bruttin, A.3    Sidoti, J.4    Constable, A.5    Fryder, V.6
  • 11
    • 0030739054 scopus 로고    scopus 로고
    • Characterization of the lysogeny DNA module from the temperate Streptococcus thermophilus bacteriophage φSfi21
    • Bruttin, A., F. Desiere, S. Lucchini, S. Foley, and H. Brüssow. 1997. Characterization of the lysogeny DNA module from the temperate Streptococcus thermophilus bacteriophage φSfi21. Virology 233:136-148.
    • (1997) Virology , vol.233 , pp. 136-148
    • Bruttin, A.1    Desiere, F.2    Lucchini, S.3    Foley, S.4    Brüssow, H.5
  • 12
    • 0041476505 scopus 로고
    • Starters for fermented milks. 3. Thermophilic starters
    • Dellaglio, F. 1988. Starters for fermented milks. 3. Thermophilic starters. Bull. Int. Dairy Fed. 227:27-33.
    • (1988) Bull. Int. Dairy Fed. , vol.227 , pp. 27-33
    • Dellaglio, F.1
  • 13
    • 0032519891 scopus 로고    scopus 로고
    • Evolution of Streptococcus thermophilus bacteriophage genomes by modular exchanges followed by point mutations and small deletions and insertions
    • Desiere, F., S. Lucchini, and H. Brüssow. 1998. Evolution of Streptococcus thermophilus bacteriophage genomes by modular exchanges followed by point mutations and small deletions and insertions. Virology 241:345-356.
    • (1998) Virology , vol.241 , pp. 345-356
    • Desiere, F.1    Lucchini, S.2    Brüssow, H.3
  • 14
    • 0030854494 scopus 로고    scopus 로고
    • A highly conserved DNA replication module from Streptococcus thermophilus phages is similar in sequence and topology to a module from Lactococcus lactis phage
    • Desiere, F., S. Lucchini, A. Bruttin, M.-C. Zwahlen, and H. Brüssow. 1997. A highly conserved DNA replication module from Streptococcus thermophilus phages is similar in sequence and topology to a module from Lactococcus lactis phage. Virology 234:372-382.
    • (1997) Virology , vol.234 , pp. 372-382
    • Desiere, F.1    Lucchini, S.2    Bruttin, A.3    Zwahlen, M.-C.4    Brüssow, H.5
  • 15
    • 0030028470 scopus 로고    scopus 로고
    • The two step lysis system of pneumococcal bacteriophage Ej-1 is functional in gram-negative bacteria: Triggering of the major pneumococcal autolysin in E. Coli
    • Díaz, E., M. Munthali, H. Lünsdorf, J. V. Höltje, and K. N. Timmis. 1996. The two step lysis system of pneumococcal bacteriophage Ej-1 is functional in gram-negative bacteria: triggering of the major pneumococcal autolysin in E. coli. Mol. Microbiol. 19:667-681.
    • (1996) Mol. Microbiol. , vol.19 , pp. 667-681
    • Díaz, E.1    Munthali, M.2    Lünsdorf, H.3    Höltje, J.V.4    Timmis, K.N.5
  • 16
    • 0342503748 scopus 로고
    • Control of phage in the dairy plant
    • Everson, T. C. 1991. Control of phage in the dairy plant. Bull. Int. Dairy Fed. 263:24-28.
    • (1991) Bull. Int. Dairy Fed. , vol.263 , pp. 24-28
    • Everson, T.C.1
  • 17
    • 84976027559 scopus 로고
    • Interactions of temperate bacteriophages of Streptococcus salivarius ssp. Thermophilus with lysogenic indicators affect phage DNA restrictions patterns and host range
    • Fayard, B., M. Haefliger, and J. P. Accolas. 1993. Interactions of temperate bacteriophages of Streptococcus salivarius ssp. thermophilus with lysogenic indicators affect phage DNA restrictions patterns and host range. J. Dairy Res. 60:385-399.
    • (1993) J. Dairy Res. , vol.60 , pp. 385-399
    • Fayard, B.1    Haefliger, M.2    Accolas, J.P.3
  • 18
    • 0025037846 scopus 로고
    • Modular organisation of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • García, P., J. L. García, E. García, J. M. Sánchez-Puelles, and R. López. 1990. Modular organisation of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86:81-88.
    • (1990) Gene , vol.86 , pp. 81-88
    • García, P.1    García, J.L.2    García, E.3    Sánchez-Puelles, J.M.4    López, R.5
  • 19
    • 0021149434 scopus 로고
    • Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: Comparative study between bacteriophage-associated lysin and the host amidase
    • García, P., E. Méndez, E. García, C. Ronda, and R. Löpez. 1984. Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: comparative study between bacteriophage-associated lysin and the host amidase. J. Bacteriol. 159:793-796.
    • (1984) J. Bacteriol. , vol.159 , pp. 793-796
    • García, P.1    Méndez, E.2    García, E.3    Ronda, C.4    Löpez, R.5
  • 20
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., D. J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 21
    • 0023055384 scopus 로고
    • Nucleotide sequence of Bacillus phage Phi29 genes 14 and 15: Homology of gene 15 with other phage lysozymes
    • Garvey, K. J., M. S. Saedi, and J. Ito. 1986. Nucleotide sequence of Bacillus phage Phi29 genes 14 and 15: homology of gene 15 with other phage lysozymes. Nucleic Acids Res. 14:10001-10008.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 10001-10008
    • Garvey, K.J.1    Saedi, M.S.2    Ito, J.3
  • 22
    • 0000395790 scopus 로고
    • Molecular genetics of bacteriophage and natural phage defence systems in the genus Lactococcus
    • Garvey, P., D. van Sinderen, D. P. Twomey, C. Hill, and G. F. Fitzgerald. 1995. Molecular genetics of bacteriophage and natural phage defence systems in the genus Lactococcus. Int. Dairy J, 5:905-947.
    • (1995) Int. Dairy J , vol.5 , pp. 905-947
    • Garvey, P.1    Van Sinderen, D.2    Twomey, D.P.3    Hill, C.4    Fitzgerald, G.F.5
  • 23
    • 0029905823 scopus 로고    scopus 로고
    • Lytic systems in lactic acid bacteria and their bacteriophages
    • Gasson, M. J. 1996. Lytic systems in lactic acid bacteria and their bacteriophages. Antonie Leeuwenhoek 10:147-159.
    • (1996) Antonie Leeuwenhoek , vol.10 , pp. 147-159
    • Gasson, M.J.1
  • 25
    • 0012136985 scopus 로고
    • The genus Streptococcus
    • B. J. B. Wood and W. H. Holzapfel (ed.), Chapman and Hall, Glasgow, United Kingdom
    • Hardie, J. M., and R. A. Whiley. 1995. The genus Streptococcus, p. 59-124. In B. J. B. Wood and W. H. Holzapfel (ed.), The lactic acid bacteria, vol. 2. The genera of lactic acid bacteria. Chapman and Hall, Glasgow, United Kingdom.
    • (1995) The Lactic Acid Bacteria, Vol. 2. The Genera of Lactic Acid Bacteria , vol.2 , pp. 59-124
    • Hardie, J.M.1    Whiley, R.A.2
  • 26
    • 0028954627 scopus 로고
    • Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage φadh
    • Henrich, B., B. Binishofer, and U. Bläsi. 1995. Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage φadh. J. Bacteriol. 177:723-732.
    • (1995) J. Bacteriol. , vol.177 , pp. 723-732
    • Henrich, B.1    Binishofer, B.2    Bläsi, U.3
  • 27
    • 0344024365 scopus 로고    scopus 로고
    • Personal communication
    • Hillier, A. J. Personal communication.
    • Hillier, A.J.1
  • 28
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofman, K., and W. Stoffel. 1993. TMbase - a database of membrane spanning proteins segments. Biol. Chem. 347:166-170.
    • (1993) Biol. Chem. , vol.347 , pp. 166-170
    • Hofman, K.1    Stoffel, W.2
  • 30
    • 0002189528 scopus 로고
    • Bacteriophages and bacteriophagc resistance
    • M. J. Gasson and W. de Vos (ed.), Blackie Academic and Professional, Glasgow, United Kingdom
    • Klaenhammer, T. R., and C. F. Fitzgerald. 1994. Bacteriophages and bacteriophagc resistance, p. 106-168. In M. J. Gasson and W. de Vos (ed.), Genetics and biotechnology of lactic acid bacteria. Blackie Academic and Professional, Glasgow, United Kingdom.
    • (1994) Genetics and Biotechnology of Lactic Acid Bacteria , pp. 106-168
    • Klaenhammer, T.R.1    Fitzgerald, C.F.2
  • 31
    • 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
  • 32
    • 0030749539 scopus 로고    scopus 로고
    • Two groups of bacteriophages infecting Streptococcus thermophilus can be distinguished on the basis of mode of packaging and genetic determinants for major structural proteins
    • Le Marrec, C., D. van Sinderen, L. Walsh, E. Stanley, E. Vlegels, S. Moineau, P. Heinze, G. Fitzgerald, and B. Fayard. 1997. Two groups of bacteriophages infecting Streptococcus thermophilus can be distinguished on the basis of mode of packaging and genetic determinants for major structural proteins. Appl. Environ. Microbiol. 63:3246-3253.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3246-3253
    • Le Marrec, C.1    Van Sinderen, D.2    Walsh, L.3    Stanley, E.4    Vlegels, E.5    Moineau, S.6    Heinze, P.7    Fitzgerald, G.8    Fayard, B.9
  • 33
    • 0032525314 scopus 로고    scopus 로고
    • The two component lysis system of Staphylococcus aureus bacteriophage Twort: A large TTG-start holin and an associated amidase endolysin
    • Loessner, M. J., S. Gaeng, G. Wendlinger, S. J. Maier, and S. Scherer. 1998. The two component lysis system of Staphylococcus aureus bacteriophage Twort: a large TTG-start holin and an associated amidase endolysin. FEMS Microbiol. Lett. 162:265-274.
    • (1998) FEMS Microbiol. Lett. , vol.162 , pp. 265-274
    • Loessner, M.J.1    Gaeng, S.2    Wendlinger, G.3    Maier, S.J.4    Scherer, S.5
  • 34
    • 0028844625 scopus 로고
    • Sequencing and analysis of the prolate-headed lactococcal bacteriophage c2 genome and identification of the structural genes
    • Lubbers, M. W., N. R. Waterfield, T. P. J. Beresford, R. W. F. Le Page, and A. W. Jarvis. 1995. Sequencing and analysis of the prolate-headed lactococcal bacteriophage c2 genome and identification of the structural genes. Appl. Environ. Microbiol. 61:4348-4356.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4348-4356
    • Lubbers, M.W.1    Waterfield, N.R.2    Beresford, T.P.J.3    Le Page, R.W.F.4    Jarvis, A.W.5
  • 35
    • 0032551191 scopus 로고    scopus 로고
    • The structural gene module in Streptococcus thermophilus bacteriophage φsfi11 shows a hierarchy of relatedness to Siphoviridae from a wide range of bacterial hosts
    • Lucchini, S., F. Desiere, and H. Brüssow. 1998. The structural gene module in Streptococcus thermophilus bacteriophage φSfi11 shows a hierarchy of relatedness to Siphoviridae from a wide range of bacterial hosts. Virology 246:63-73.
    • (1998) Virology , vol.246 , pp. 63-73
    • Lucchini, S.1    Desiere, F.2    Brüssow, H.3
  • 36
    • 0031912599 scopus 로고    scopus 로고
    • Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells
    • Martín, A. C., R. López, and P. García. 1998. Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells. J. Bacteriol. 180:210-217.
    • (1998) J. Bacteriol. , vol.180 , pp. 210-217
    • Martín, A.C.1    López, R.2    García, P.3
  • 37
    • 0029940995 scopus 로고    scopus 로고
    • Analysis of the complete nucleotide sequence and functional organization of the genome of Streptococcus pneumoniae bacteriophage Cp-1
    • Martín, A. C., R. López, and P. García. 1996. Analysis of the complete nucleotide sequence and functional organization of the genome of Streptococcus pneumoniae bacteriophage Cp-1. J. Virol. 70:3678-3687.
    • (1996) J. Virol. , vol.70 , pp. 3678-3687
    • Martín, A.C.1    López, R.2    García, P.3
  • 38
    • 0023975007 scopus 로고
    • Present state of lactic acid bacteria phage taxonomy
    • Mata, M., and P. Ritzenthaler. 1988. Present state of lactic acid bacteria phage taxonomy. Biochimie 70:395-399.
    • (1988) Biochimie , vol.70 , pp. 395-399
    • Mata, M.1    Ritzenthaler, P.2
  • 40
    • 0024558394 scopus 로고
    • Classification of virulent bacteriophages of Streptococcus salivarius subsp. Thermophilus isolated from yogurt and Swiss-type cheese
    • Neve, H., U. Krusch, and M. Teuber. 1989. Classification of virulent bacteriophages of Streptococcus salivarius subsp. thermophilus isolated from yogurt and Swiss-type cheese. Appl. Microbiol. Biotechnol. 30:624-629.
    • (1989) Appl. Microbiol. Biotechnol. , vol.30 , pp. 624-629
    • Neve, H.1    Krusch, U.2    Teuber, M.3
  • 41
    • 0032004892 scopus 로고    scopus 로고
    • Comparison of the lysogeny modules from the temperate Streptococcus thermophilus bacteriophages TP-J34 and φSfi21: Implications for the modular theory of phage evolution
    • Neve, H., K. I. Zenz, F. Desiere, A. Koch, K. J. Heller, and H. Brüssow. 1998. Comparison of the lysogeny modules from the temperate Streptococcus thermophilus bacteriophages TP-J34 and φSfi21: implications for the modular theory of phage evolution. Virology 241:61-72.
    • (1998) Virology , vol.241 , pp. 61-72
    • Neve, H.1    Zenz, K.I.2    Desiere, F.3    Koch, A.4    Heller, K.J.5    Brüssow, H.6
  • 42
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 43
  • 44
    • 0026641226 scopus 로고
    • Location, characterisation and expression of the lytic enzyme encoding gene, lytA, of Lactococcus lactis bacteriophage φUS3
    • Platteeuw, C., and W. M. de Vos. 1992. Location, characterisation and expression of the lytic enzyme encoding gene, lytA, of Lactococcus lactis bacteriophage φUS3. Gene 118:115-120.
    • (1992) Gene , vol.118 , pp. 115-120
    • Platteeuw, C.1    De Vos, W.M.2
  • 45
    • 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. 214:214-218.
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 214-218
    • Potvin, C.1    Leclerc, D.2    Tremblay, G.3    Asselin, A.4    Bellemare, G.5
  • 46
    • 0028920981 scopus 로고
    • The lysins of bacteriophages infecting lactic acid bacteria
    • Sable, S., and S. Lortal. 1995. The lysins of bacteriophages infecting lactic acid bacteria. Appl. Microbiol. Biotechnol. 43:1-6.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 1-6
    • Sable, S.1    Lortal, S.2
  • 48
    • 0028020677 scopus 로고
    • Sequence and organisation of the lactococcal prolate-headed bIL67 phage genome
    • Schouler, C., S. D. Erlich, and M. C. Chopin. 1994. Sequence and organisation of the lactococcal prolate-headed bIL67 phage genome. Microbiology 140:3061-3069.
    • (1994) Microbiology , vol.140 , pp. 3061-3069
    • Schouler, C.1    Erlich, S.D.2    Chopin, M.C.3
  • 50
    • 0027931703 scopus 로고
    • Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes
    • Shearman, C. A., K. L. Jury, and M. J. Gasson. 1994. Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes. Appl. Environ. Microbiol. 60:3063-3073.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3063-3073
    • Shearman, C.A.1    Jury, K.L.2    Gasson, M.J.3
  • 52
    • 0030824227 scopus 로고    scopus 로고
    • The lytic enzyme of the pneumococcal phage Dp-1: A chimeric lysin of intergeneric origin
    • Sheehan, M. M., J. L. García, R. López, and P. García. 1997. The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. Mol. Microbiol. 25:717-725.
    • (1997) Mol. Microbiol. , vol.25 , pp. 717-725
    • Sheehan, M.M.1    García, J.L.2    López, R.3    García, P.4
  • 53
    • 0029906313 scopus 로고    scopus 로고
    • Analysis of the catalytic domain of the lysin of the lactococcal bacteriophage Tuc2009 by chimeric gene assembling
    • Sheehan, M. M., J. L. García, R. López, and P. García. 1996. Analysis of the catalytic domain of the lysin of the lactococcal bacteriophage Tuc2009 by chimeric gene assembling. FEMS Microbiol. Lett. 140:23-28.
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 23-28
    • Sheehan, M.M.1    García, J.L.2    López, R.3    García, P.4
  • 54
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of E. Coli 16S rRNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of E. coli 16S rRNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 55
    • 0030984605 scopus 로고    scopus 로고
    • Cloning and sequencing of zooA, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin
    • Simmonds, R. S., W. J. Simpson, and J. R. Tagg. 1997. Cloning and sequencing of zooA, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin. Gene 189:255-261.
    • (1997) Gene , vol.189 , pp. 255-261
    • Simmonds, R.S.1    Simpson, W.J.2    Tagg, J.R.3
  • 56
    • 0029909725 scopus 로고    scopus 로고
    • Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881
    • Simmonds, R. S., L. Pearson, R. C. Kennedy, and J. R. Tagg. 1996. Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881. Appl. Environ. Microbiol. 62:4536-4541.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4536-4541
    • Simmonds, R.S.1    Pearson, L.2    Kennedy, R.C.3    Tagg, J.R.4
  • 57
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 59
    • 0030723809 scopus 로고    scopus 로고
    • Sequence analysis and characterisation of φo1205, a temperate bacteriophage infecting Streptococcus thermophilus CNRZ1205
    • Stanley, E., G. F. Fitzgerald, C. LeMarrec, B. Fayard, and D. van Sinderen. 1997. Sequence analysis and characterisation of φO1205, a temperate bacteriophage infecting Streptococcus thermophilus CNRZ1205. Microbiology 143:3417-3429.
    • (1997) Microbiology , vol.143 , pp. 3417-3429
    • Stanley, E.1    Fitzgerald, G.F.2    LeMarrec, C.3    Fayard, B.4    Van Sinderen, D.5
  • 60
    • 0027211113 scopus 로고
    • Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105
    • Steiner, M., and U. Bläsi. 1993. Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105. Mol. Microbiol. 8:525-533.
    • (1993) Mol. Microbiol. , vol.8 , pp. 525-533
    • Steiner, M.1    Bläsi, U.2
  • 61
    • 0027528507 scopus 로고
    • The missing link in the phage lysis of gram-positive bacteria: Gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein
    • Steiner, M., W. Lubitz, and U. Bläsi. 1993. The missing link in the phage lysis of gram-positive bacteria: gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein. J. Bacteriol. 175:1038-1042.
    • (1993) J. Bacteriol. , vol.175 , pp. 1038-1042
    • Steiner, M.1    Lubitz, W.2    Bläsi, U.3
  • 62
    • 0016686551 scopus 로고
    • Improved media for lactic streptococci and their bacteriophages
    • Terzaghi, B. E., and W. E. Sandine. 1975. Improved media for lactic streptococci and their bacteriophages. Appl. Microbiol. 29:807-813.
    • (1975) Appl. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 63
    • 0028799370 scopus 로고
    • Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. Lactis bacteriophage LL-H lysin
    • Vasala, A., M. Välkkilä, J. Caldentey, and T. Alatossava. 1995. Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin. Appl. Environ. Microbiol. 61:4004-4011.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4004-4011
    • Vasala, A.1    Välkkilä, M.2    Caldentey, J.3    Alatossava, T.4
  • 64
    • 0025778673 scopus 로고
    • Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity
    • Wang, X., B. J. Wilkinson, and R. K. Jayaswal. 1991. Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Gene 102:105-109.
    • (1991) Gene , vol.102 , pp. 105-109
    • Wang, X.1    Wilkinson, B.J.2    Jayaswal, R.K.3
  • 65
  • 66
    • 0028882367 scopus 로고
    • Sequence analysis of the region upstream of a peptidoglycan hvdrolase-encoding gene from bacteriophage φ11 of Staphylococcus aureus
    • Weerakoon, L. K., and R. K. Jayaswal. 1995. Sequence analysis of the region upstream of a peptidoglycan hvdrolase-encoding gene from bacteriophage φ11 of Staphylococcus aureus. FEMS Microbiol. Lett. 133:9-15.
    • (1995) FEMS Microbiol. Lett. , vol.133 , pp. 9-15
    • Weerakoon, L.K.1    Jayaswal, R.K.2
  • 67
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • Young, R. 1992. Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56:430-481.
    • (1992) Microbiol. Rev. , vol.56 , pp. 430-481
    • Young, R.1
  • 68
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young, R., and U. Bläsi. 1995. Holins: form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 191-205
    • Young, R.1    Bläsi, U.2
  • 69
    • 0028100794 scopus 로고
    • Functions involved in bacteriophage P2-induced host cell lysis and identification of a new tail gene
    • Ziermann, R., B. Bartlett, R. Calendar, and G. E. Christie. 1994. Functions involved in bacteriophage P2-induced host cell lysis and identification of a new tail gene. J. Bacteriol. 176:4974-4984.
    • (1994) J. Bacteriol. , vol.176 , pp. 4974-4984
    • Ziermann, R.1    Bartlett, B.2    Calendar, R.3    Christie, G.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.