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Volumn 151, Issue 7, 2005, Pages 2331-2342

Functional analysis of the lysis genes of Staphylococcus aureus phage P68 in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DOUBLE STRANDED DNA;

EID: 22144453870     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.27937-0     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0344863179 scopus 로고    scopus 로고
    • The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1
    • Alonso, J. C., Luder, G., Stiege, A. C., Chai, S., Weise, F. & Trautner, T. A. (1997). The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1. Gene 204, 201-212.
    • (1997) Gene , vol.204 , pp. 201-212
    • Alonso, J.C.1    Luder, G.2    Stiege, A.C.3    Chai, S.4    Weise, F.5    Trautner, T.A.6
  • 2
    • 0033043978 scopus 로고    scopus 로고
    • Characterization of the dual start motif of a class II holin gene
    • Barenboim, M., Chang, C. Y., Hajj, F. & Young, R. (1999). Characterization of the dual start motif of a class II holin gene. Mol Microbiol 32, 715-727.
    • (1999) Mol. Microbiol. , vol.32 , pp. 715-727
    • Barenboim, M.1    Chang, C.Y.2    Hajj, F.3    Young, R.4
  • 3
    • 0036035524 scopus 로고    scopus 로고
    • Breaking free: "Protein antibiotics" and phage lysis
    • Bernhart, T. G., Wang, I. N., Struck, D. K. & Young, R. (2002). Breaking free: "protein antibiotics" and phage lysis. Res Microbiol 153, 493-501.
    • (2002) Res. Microbiol. , vol.153 , pp. 493-501
    • Bernhart, T.G.1    Wang, I.N.2    Struck, D.K.3    Young, R.4
  • 4
    • 0029764787 scopus 로고    scopus 로고
    • Two beginnings for a single purpose: The dual-start holins in the regulation of phage lysis
    • Bläsi, U. & Young, R. (1996). Two beginnings for a single purpose: the dual-start holins in the regulation of phage lysis. Mol Microbiol 21, 675-682.
    • (1996) Mol. Microbiol. , vol.21 , pp. 675-682
    • Bläsi, U.1    Young, R.2
  • 5
    • 0024422744 scopus 로고
    • Dual translational initiation sites control function of the lambda S gene
    • Bläsi, U., Nam, K., Hartz, D., Gold, L. & Young, R. (1989). Dual translational initiation sites control function of the lambda S gene. EMBO J 8, 3501-3510.
    • (1989) EMBO J. , vol.8 , pp. 3501-3510
    • Bläsi, U.1    Nam, K.2    Hartz, D.3    Gold, L.4    Young, R.5
  • 6
    • 0025317560 scopus 로고
    • The lethal lambda S gene encodes its own inhibitor
    • Bläsi, U., Chang, C. Y., Zagotte, M. T., Nam, K. & Young, R. (1990). The lethal lambda S gene encodes its own inhibitor. EMBO J 9, 981-989.
    • (1990) EMBO J. , vol.9 , pp. 981-989
    • Bläsi, U.1    Chang, C.Y.2    Zagotte, M.T.3    Nam, K.4    Young, R.5
  • 7
    • 0030739054 scopus 로고    scopus 로고
    • Characterization of the lysogeny module from the temperate Streptococcus thermophilus bacteriophage Sfi21
    • Bruttin, A., Desiere, F., Lucchini, S., Foley, S. & Brüssow, H. (1997). Characterization of the lysogeny module from the temperate Streptococcus thermophilus bacteriophage Sfi21. 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
  • 8
    • 0029020763 scopus 로고
    • S gene expression and the timing of lysis by bacteriophage lambda
    • Chang, C.-Y., Nam, K. & Young, R. (1995). S gene expression and the timing of lysis by bacteriophage lambda. J Bacteriol 177, 3283-3294.
    • (1995) J. Bacteriol. , vol.177 , pp. 3283-3294
    • Chang, C.-Y.1    Nam, K.2    Young, R.3
  • 10
    • 0037903426 scopus 로고    scopus 로고
    • Novel method to control pathogenic bacteria on human mucous membranes
    • Fischetti, V. A. (2003). Novel method to control pathogenic bacteria on human mucous membranes. Ann N Y Acad Sci 987, 207-214.
    • (2003) Ann. N Y Acad. Sci. , vol.987 , pp. 207-214
    • Fischetti, V.A.1
  • 11
    • 0023197916 scopus 로고
    • Cloning, purification, and biochemical characterization of the pneumococcal bacteriophage Cp-1 lysin
    • García, J. L., García, E., Arrarás, A., García, P., Ronda, C. & López, R. (1987). Cloning, purification, and biochemical characterization of the pneumococcal bacteriophage Cp-1 lysin. J Virol 61, 2573-2580.
    • (1987) J. Virol. , vol.61 , pp. 2573-2580
    • García, J.L.1    García, E.2    Arrarás, A.3    García, P.4    Ronda, C.5    López, R.6
  • 12
    • 0020372980 scopus 로고
    • Lethal action of bacteriophage lambda S gene
    • Garrett, J. M. & Young, R. (1982). Lethal action of bacteriophage lambda S gene. J Virol 44, 886-892.
    • (1982) J. Virol. , vol.44 , pp. 886-892
    • Garrett, J.M.1    Young, R.2
  • 13
    • 0033020341 scopus 로고    scopus 로고
    • Molecular analysis of the region encoding the lytic system from Oenococcus oeni temperate bacteriophage φ 10MC
    • Gindreau, E. & Lonvaud-Funel, A. (1999). Molecular analysis of the region encoding the lytic system from Oenococcus oeni temperate bacteriophage φ 10MC. FEMS Microbiol Lett 219, 275-283.
    • (1999) FEMS Microbiol. Lett. , vol.219 , pp. 275-283
    • Gindreau, E.1    Lonvaud-Funel, A.2
  • 14
    • 0032767883 scopus 로고    scopus 로고
    • Molecular function of the dual start motif in the lambda S holin
    • Graschopf, A. & Bläsi, U. (1999). Molecular function of the dual start motif in the lambda S holin. Mol Microbiol 33, 569-582.
    • (1999) Mol. Microbiol. , vol.33 , pp. 569-582
    • Graschopf, A.1    Bläsi, U.2
  • 15
    • 0033758938 scopus 로고    scopus 로고
    • Dimerization between the holin and holin inhibitor of phage lambda
    • Gründling, A., Smith, D. L., Bläsi, U. & Young, R. (2000). Dimerization between the holin and holin inhibitor of phage lambda. J Bacteriol 182, 6075-6081.
    • (2000) J. Bacteriol. , vol.182 , pp. 6075-6081
    • Gründling, A.1    Smith, D.L.2    Bläsi, U.3    Young, R.4
  • 17
    • 0026033684 scopus 로고
    • Influence of mRNA determinants on translation initiation in Escherichia coli
    • Hartz, D., McPheeters, D. S. & Gold, L. (1991). Influence of mRNA determinants on translation initiation in Escherichia coli. J Mol Biol 218, 83-97.
    • (1991) J. Mol. Biol. , vol.218 , pp. 83-97
    • Hartz, D.1    McPheeters, D.S.2    Gold, L.3
  • 18
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K. & Stoffel, W. (1993). TMbase - a database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 374, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 19
    • 0025113017 scopus 로고
    • Construction of vectors with the p15a replicon, kanamycin resistance, inducible lacZα and pUC18 or pUC19 multiple cloning sites
    • Jobling, M. G. & Holmes, R. K. (1990). Construction of vectors with the p15a replicon, kanamycin resistance, inducible lacZα and pUC18 or pUC19 multiple cloning sites. Nucleic Acids Res 18, 5315-5316.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5315-5316
    • Jobling, M.G.1    Holmes, R.K.2
  • 20
    • 0031925095 scopus 로고    scopus 로고
    • Lysis genes of the Bacillus subtilis defective prophage PBSX
    • Krogh, S., Jørgensen, S. T. & Devine, K. M. (1998). Lysis genes of the Bacillus subtilis defective prophage PBSX. J Bacteriol 180, 2110-2117.
    • (1998) J. Bacteriol. , vol.180 , pp. 2110-2117
    • Krogh, S.1    Jørgensen, S.T.2    Devine, K.M.3
  • 21
    • 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
  • 22
    • 0345077411 scopus 로고
    • Promoters largely determine the efficiency of repressor action
    • Lanzer, M. & Bujard, H. (1988). Promoters largely determine the efficiency of repressor action. Proc Natl Acad Sci U S A 85, 8973-8977.
    • (1988) Proc. Natl. Acad. Sci. U S A , vol.85 , pp. 8973-8977
    • Lanzer, M.1    Bujard, H.2
  • 23
    • 0031793330 scopus 로고    scopus 로고
    • Analysis of the bacteriolytic enzymes of the autolytic Lactococcus lactis subsp. cremoris strain AM2 by renaturing polyacrylamide gel electrophoresis: Identification of a prophage-encoded enzyme
    • Lepeuple, A. S., Van Gemert, E. & Chapot-Chartier, M. P. (1998). Analysis of the bacteriolytic enzymes of the autolytic Lactococcus lactis subsp. cremoris strain AM2 by renaturing polyacrylamide gel electrophoresis: identification of a prophage-encoded enzyme. Appl Environ Microbiol 64, 4142-4148.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4142-4148
    • Lepeuple, A.S.1    Van Gemert, E.2    Chapot-Chartier, M.P.3
  • 24
    • 0242286566 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia
    • Loeffler, J. M., Djurkovic, S. & Fischetti, V. A. (2003). Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect Immun 71, 6199-6204.
    • (2003) Infect. Immun. , vol.71 , pp. 6199-6204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 25
    • 0028963469 scopus 로고
    • A new procedure for efficient recovery of DNA, RNA, and proteins from Listeria cells by rapid lysis with a recombinant bacteriophage endolysin
    • Loessner, M. J., Schneider, A. & Scherer, S. (1995). A new procedure for efficient recovery of DNA, RNA, and proteins from Listeria cells by rapid lysis with a recombinant bacteriophage endolysin. Appl Environ Microbiol 61, 1150-1152.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1150-1152
    • Loessner, M.J.1    Schneider, A.2    Scherer, S.3
  • 26
    • 0030894847 scopus 로고    scopus 로고
    • Three Bacillus cereus bacteriophage endolysins are unrelated but reveal homology to cell wall hydrolases from different bacilli
    • Loessner, M. J., Maier, S. K., Daubek-Puza, H., Wendlinger, G. & Scherer, S. (1997). Three Bacillus cereus bacteriophage endolysins are unrelated but reveal homology to cell wall hydrolases from different bacilli. J Bacteriol 179, 2845-2851.
    • (1997) J. Bacteriol. , vol.179 , pp. 2845-2851
    • Loessner, M.J.1    Maier, S.K.2    Daubek-Puza, H.3    Wendlinger, G.4    Scherer, S.5
  • 27
    • 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., Gaeng, S., Wendlinger, G., Maier, S. K. & Scherer, S. (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.K.4    Scherer, S.5
  • 28
    • 0032809133 scopus 로고    scopus 로고
    • Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187
    • Loessner, M. J., Gaeng, S. & Scherer, S. (1999). Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187. J Bacteriol 181, 4452-4460.
    • (1999) J. Bacteriol. , vol.181 , pp. 4452-4460
    • Loessner, M.J.1    Gaeng, S.2    Scherer, S.3
  • 29
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy, F. D. (1998). Staphylococcus aureus infections. N Engl J Med 339, 520-532.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 30
    • 0034072572 scopus 로고    scopus 로고
    • Identification, cloning, and initial characterization of rot, a locus encoding a regulator of virulence factor expression in Staphylococcus aureus
    • McNamara, P. J., Milligan-Monroe, K. C., Khalili, S. & Proctor, R. A. (2000). Identification, cloning, and initial characterization of rot, a locus encoding a regulator of virulence factor expression in Staphylococcus aureus. J Bacteriol 182, 3197-3203.
    • (2000) J. Bacteriol. , vol.182 , pp. 3197-3203
    • McNamara, P.J.1    Milligan-Monroe, K.C.2    Khalili, S.3    Proctor, R.A.4
  • 31
    • 0033026268 scopus 로고    scopus 로고
    • Multiple enzymatic activities of the murein hydrolase from Staphylococcal phage φ11
    • Navarre, W. W., Ton-That, H., Faull, K. F. & Schneewind O. (1999). Multiple enzymatic activities of the murein hydrolase from Staphylococcal phage φ11. J Biol Chem 274, 15847-15856.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15847-15856
    • Navarre, W.W.1    Ton-That, H.2    Faull, K.F.3    Schneewind, O.4
  • 32
    • 0023622282 scopus 로고
    • Highly repressible expression system for cloning genes that specify potentially toxic proteins
    • O'Connor, C. D. & Timmis, K. N. (1987). Highly repressible expression system for cloning genes that specify potentially toxic proteins. J Bacteriol 169, 4457-4462.
    • (1987) J. Bacteriol. , vol.169 , pp. 4457-4462
    • O'Connor, C.D.1    Timmis, K.N.2
  • 33
    • 0344958845 scopus 로고    scopus 로고
    • Gene organization in a central DNA fragment of Oenococcus oeni bacteriophage fOg44 encoding lytic, integrative and non-essential functions
    • Parreira, R., Sao-Jose, C., Isidro, A., Domingues, S., Vieira, G. & Santos, M. A. (1999). Gene organization in a central DNA fragment of Oenococcus oeni bacteriophage fOg44 encoding lytic, integrative and non-essential functions. Gene 226, 83-93.
    • (1999) Gene , vol.226 , pp. 83-93
    • Parreira, R.1    Sao-Jose, C.2    Isidro, A.3    Domingues, S.4    Vieira, G.5    Santos, M.A.6
  • 34
    • 0024101177 scopus 로고
    • Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli
    • Potvin, C., Leclerc, D., Tremblay, G., Asselin, A. & Bellamare, G. (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    Bellamare, G.5
  • 35
    • 0021891846 scopus 로고
    • Phage P22 lysis genes: Nucleotide sequences and functional relationships with T4 and lambda genes
    • Rennell, D. & Poteete, A. R. (1985). Phage P22 lysis genes: nucleotide sequences and functional relationships with T4 and lambda genes. Virology 143, 280-289.
    • (1985) Virology , vol.143 , pp. 280-289
    • Rennell, D.1    Poteete, A.R.2
  • 37
    • 0027931703 scopus 로고
    • Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes
    • Shearman, C., Jury, K. & Gasson, M. J. (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.1    Jury, K.2    Gasson, M.J.3
  • 38
    • 0032976001 scopus 로고    scopus 로고
    • Identification and characterization of a lysis module present in a large proportion of bacteriophages infecting Streptococcus thermophilus
    • Sheehan, M. M., Stanley, E., Fitzgerald, G. F. & van Sinderen, D. (1999). Identification and characterization of a lysis module present in a large proportion of bacteriophages infecting Streptococcus thermophilus. Appl Environ Microbiol 65, 569-577.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 569-577
    • Sheehan, M.M.1    Stanley, E.2    Fitzgerald, G.F.3    van Sinderen, D.4
  • 39
    • 0027211113 scopus 로고
    • Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105
    • Steiner, M. & Bläsi, U. (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
  • 40
    • 0027528507 scopus 로고
    • The missing link in phage lysis of gram-positive bacteria: Gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein
    • Steiner, M., Lubitz, W. & Bläsi, U. (1993). The missing link in 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
  • 41
    • 0037469628 scopus 로고    scopus 로고
    • Complete nucleotide sequence and molecular characterization of two lytic Staphylococcus aureus phages: 44AHJD and P68
    • Vybiral, D., Takáč, M., Loessner, M., Witte, A., von Ahsen, U. & Bläsi, U. (2003). Complete nucleotide sequence and molecular characterization of two lytic Staphylococcus aureus phages: 44AHJD and P68. FEMS Microbiol Lett 219, 275-283.
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 275-283
    • Vybiral, D.1    Takáč, M.2    Loessner, M.3    Witte, A.4    von Ahsen, U.5    Bläsi, U.6
  • 42
    • 0025778673 scopus 로고
    • Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity
    • Wang, X., Wilkinson, B. J. & Jayaswal, R. K. (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
  • 43
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang, I. N., Smith, D. L. & Young, R. (2000). Holins: the protein clocks of bacteriophage infections. Annu Rev Microbiol 54, 799-825.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 44
    • 0037310365 scopus 로고    scopus 로고
    • Sizing the holin lesion with an endolysin-beta-galactosidase fusion
    • Wang, I. N., Deaton, J. & Young, R. (2003). Sizing the holin lesion with an endolysin-beta-galactosidase fusion. J Bacteriol 185, 779-787.
    • (2003) J. Bacteriol. , vol.185 , pp. 779-787
    • Wang, I.N.1    Deaton, J.2    Young, R.3
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 46
    • 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
  • 47
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young, R. & Bläsi, U. (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
  • 48
    • 0034162940 scopus 로고    scopus 로고
    • Phages will out: Strategies of host cell lysis
    • Young, R., Wang, I. N. & Roof, W. D. (2000). Phages will out: strategies of host cell lysis. Trends Microbiol 8, 120-128.
    • (2000) Trends Microbiol. , vol.8 , pp. 120-128
    • Young, R.1    Wang, I.N.2    Roof, W.D.3
  • 49
    • 0025019776 scopus 로고
    • Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli
    • Zagotta, M. T. & Wilson, D. B. (1990). Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli. J Bacteriol 172, 912-921.
    • (1990) J. Bacteriol. , vol.172 , pp. 912-921
    • Zagotta, M.T.1    Wilson, D.B.2
  • 50
    • 0036840423 scopus 로고    scopus 로고
    • The murein hydrolase of the bacteriophage Phi3626 dual lysis system is active against all tested Clostridium perfringens strains
    • Zimmer, M., Vukov, N., Scherer, S. & Loessner, M. J. (2002). The murein hydrolase of the bacteriophage Phi3626 dual lysis system is active against all tested Clostridium perfringens strains. Appl Environ Microbiol 68, 5311-5317.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5311-5317
    • Zimmer, M.1    Vukov, N.2    Scherer, S.3    Loessner, M.J.4


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