메뉴 건너뛰기




Volumn 7, Issue 2, 2012, Pages

A T3 and T7 recombinant phage acquires efficient adsorption and a broader host range

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DEOXYRIBONUCLEASE I; DNA FRAGMENT;

EID: 84863036350     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030954     Document Type: Article
Times cited : (60)

References (50)
  • 1
    • 0001754802 scopus 로고
    • The T7 group
    • In: Calendar R, editors, New York, NY, Plenum press
    • Hausmann R, (1988) The T7 group. In: Calendar R, editors. Bacteriophages vol.1 New York, NY Plenum press pp. 259-289.
    • (1988) Bacteriophages Vol.1 , pp. 259-289
    • Hausmann, R.1
  • 2
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn JJ, Studier FW, (1983) Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J Mol Biol 166: 477-535.
    • (1983) J Mol Biol , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 3
    • 0036300881 scopus 로고    scopus 로고
    • Complete nucleotide sequence and likely recombinatorial origin of bacteriophage T3
    • Pajunen MI, Elizondo MR, Skurnik M, Kieleczawa J, Molineux IJ, (2002) Complete nucleotide sequence and likely recombinatorial origin of bacteriophage T3. J Mol Biol 319: 1115-1132.
    • (2002) J Mol Biol , vol.319 , pp. 1115-1132
    • Pajunen, M.I.1    Elizondo, M.R.2    Skurnik, M.3    Kieleczawa, J.4    Molineux, I.J.5
  • 4
    • 0015223571 scopus 로고
    • A study in evolution: the DNA base sequence homology between coliphages T7 and T3
    • Davis RW, Hyman RW, (1971) A study in evolution: the DNA base sequence homology between coliphages T7 and T3. J Mol Biol 62: 287-301.
    • (1971) J Mol Biol , vol.62 , pp. 287-301
    • Davis, R.W.1    Hyman, R.W.2
  • 5
    • 0024324129 scopus 로고
    • Synthesis of the capsid protein inhibits development of bacteriophage T3 mutants that abortively infect F plasmid-containing cells
    • Condreay JP, Molineux IJ, (1989) Synthesis of the capsid protein inhibits development of bacteriophage T3 mutants that abortively infect F plasmid-containing cells. J Mol Biol 207: 543-554.
    • (1989) J Mol Biol , vol.207 , pp. 543-554
    • Condreay, J.P.1    Molineux, I.J.2
  • 6
    • 0018380111 scopus 로고
    • Relationships among different strains of T7 and among T7-related bacteriophages
    • Studier FW, (1979) Relationships among different strains of T7 and among T7-related bacteriophages. Virology 95: 70-84.
    • (1979) Virology , vol.95 , pp. 70-84
    • Studier, F.W.1
  • 7
    • 0017156121 scopus 로고
    • SAMase gene of bacteriophage T3 is responsible for overcoming host restriction
    • Studier FW, Movva NR, (1976) SAMase gene of bacteriophage T3 is responsible for overcoming host restriction. J Virol 19: 136-145.
    • (1976) J Virol , vol.19 , pp. 136-145
    • Studier, F.W.1    Movva, N.R.2
  • 8
    • 0015229875 scopus 로고
    • Different template specificities of phage T3 and T7 RNA polymerases
    • Dunn JJ, Bautz FA, Bautz EK, (1971) Different template specificities of phage T3 and T7 RNA polymerases. Nat New Biol 230: 94-96.
    • (1971) Nat New Biol , vol.230 , pp. 94-96
    • Dunn, J.J.1    Bautz, F.A.2    Bautz, E.K.3
  • 9
    • 0014119419 scopus 로고
    • Amber mutants of bacteriophages T3 and T7 defective in phage-directed deoxyribonucleic acid synthesis
    • Hausmann R, Gomez B, (1967) Amber mutants of bacteriophages T3 and T7 defective in phage-directed deoxyribonucleic acid synthesis. J Virol 1: 779-792.
    • (1967) J Virol , vol.1 , pp. 779-792
    • Hausmann, R.1    Gomez, B.2
  • 10
    • 0016335059 scopus 로고
    • T3 times T7 phage crosses leading to recombinant RNA polymerases
    • Beier H, Hausmann R, (1974) T3 times T7 phage crosses leading to recombinant RNA polymerases. Nature 251: 538-540.
    • (1974) Nature , vol.251 , pp. 538-540
    • Beier, H.1    Hausmann, R.2
  • 11
    • 0017344960 scopus 로고
    • Isolation of recombinants between T7 and T3 bacteriophages and their use in vitro transcriptional mapping
    • Beier H, Golomb M, Chamberlin M, (1977) Isolation of recombinants between T7 and T3 bacteriophages and their use in vitro transcriptional mapping. J Virol 21: 753-765.
    • (1977) J Virol , vol.21 , pp. 753-765
    • Beier, H.1    Golomb, M.2    Chamberlin, M.3
  • 12
    • 0022999280 scopus 로고
    • Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity
    • Huber HE, Russel M, Model P, Richardson CC, (1986) Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity. J Biol Chem 261: 15006-15012.
    • (1986) J Biol Chem , vol.261 , pp. 15006-15012
    • Huber, H.E.1    Russel, M.2    Model, P.3    Richardson, C.C.4
  • 13
    • 0034095350 scopus 로고    scopus 로고
    • Repair of double-strand breaks by incorporation of a molecule of homologous DNA
    • Lai YT, Masker W, (2000) Repair of double-strand breaks by incorporation of a molecule of homologous DNA. Mol Microbiol 36: 437-446.
    • (2000) Mol Microbiol , vol.36 , pp. 437-446
    • Lai, Y.T.1    Masker, W.2
  • 14
    • 0035108124 scopus 로고    scopus 로고
    • T7 single strand DNA binding protein but not T7 helicase is required for DNA double strand break repair
    • Yu M, Masker W, (2001) T7 single strand DNA binding protein but not T7 helicase is required for DNA double strand break repair. J Bacteriol 183: 1862-1869.
    • (2001) J Bacteriol , vol.183 , pp. 1862-1869
    • Yu, M.1    Masker, W.2
  • 15
    • 0016680394 scopus 로고
    • The involvement of genes 3,4,5 and 6 in genetic recombination in bacteriophage T7
    • Kerr C, Sadowski PD, (1975) The involvement of genes 3,4,5 and 6 in genetic recombination in bacteriophage T7. Virology 65: 281-285.
    • (1975) Virology , vol.65 , pp. 281-285
    • Kerr, C.1    Sadowski, P.D.2
  • 16
    • 0016301438 scopus 로고
    • Some functions involved in bacteriophage T7 genetic recombination
    • Powling A, Knippers R, (1974) Some functions involved in bacteriophage T7 genetic recombination. Mol Gen Genet 134: 173-180.
    • (1974) Mol Gen Genet , vol.134 , pp. 173-180
    • Powling, A.1    Knippers, R.2
  • 17
    • 0019410374 scopus 로고
    • The participation of T7 DNA-binding protein in T7 genetic recombination
    • Araki H, Ogawa H, (1981) The participation of T7 DNA-binding protein in T7 genetic recombination. Virology 111: 509-515.
    • (1981) Virology , vol.111 , pp. 509-515
    • Araki, H.1    Ogawa, H.2
  • 18
    • 33745721355 scopus 로고
    • The physical properties of T7 bacteriophage
    • Davison PF, Freifelder D, (1962) The physical properties of T7 bacteriophage. J Mol Biol 5: 635-642.
    • (1962) J Mol Biol , vol.5 , pp. 635-642
    • Davison, P.F.1    Freifelder, D.2
  • 19
    • 0021727529 scopus 로고
    • Molecular analysis of F plasmid pif region specifying abortive infection of T7 phage
    • Cram D, Ray A, Skurray R, (1984) Molecular analysis of F plasmid pif region specifying abortive infection of T7 phage. Mol Gen Genet 197: 137-142.
    • (1984) Mol Gen Genet , vol.197 , pp. 137-142
    • Cram, D.1    Ray, A.2    Skurray, R.3
  • 20
    • 0026090245 scopus 로고
    • Expression of gene 1.2 and gene 10 of bacteriophage T7 is lethal to F plasmid-containing Escherichia coli
    • Schmitt CK, Molineux IJ, (1991) Expression of gene 1.2 and gene 10 of bacteriophage T7 is lethal to F plasmid-containing Escherichia coli. J Bacteriol 173: 1536-1543.
    • (1991) J Bacteriol , vol.173 , pp. 1536-1543
    • Schmitt, C.K.1    Molineux, I.J.2
  • 21
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T, (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391: 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 22
    • 0024353628 scopus 로고
    • Nucleotide sequence and complementation studies of the gene 10 region of bacteriophage T3
    • Condreay JP, Wright SE, Molineux IJ, (1989) Nucleotide sequence and complementation studies of the gene 10 region of bacteriophage T3. J Mol Biol 207: 555-561.
    • (1989) J Mol Biol , vol.207 , pp. 555-561
    • Condreay, J.P.1    Wright, S.E.2    Molineux, I.J.3
  • 23
    • 0005163336 scopus 로고
    • Bacterial viruses; with particular reference to adsorption/penetration
    • Weidel W, (1958) Bacterial viruses; with particular reference to adsorption/penetration. Annu Rev Microbiol 12: 27-48.
    • (1958) Annu Rev Microbiol , vol.12 , pp. 27-48
    • Weidel, W.1
  • 24
    • 0024292372 scopus 로고
    • Molecular substructure of a viral receptor-recognition protein. The gp17 tail-fiber of bacteriophage T7
    • Steven AC, Trus BL, Maizel JV, Unser M, Parry DA, et al. (1988) Molecular substructure of a viral receptor-recognition protein. The gp17 tail-fiber of bacteriophage T7. J Mol Biol 200: 351-365.
    • (1988) J Mol Biol , vol.200 , pp. 351-365
    • Steven, A.C.1    Trus, B.L.2    Maizel, J.V.3    Unser, M.4    Parry, D.A.5
  • 25
    • 0021676950 scopus 로고
    • Purification and properties of gene 18 product of bacteriophage T3
    • Hamada K, Fujisawa H, Minagawa T, (1984) Purification and properties of gene 18 product of bacteriophage T3. Virology 139: 251-259.
    • (1984) Virology , vol.139 , pp. 251-259
    • Hamada, K.1    Fujisawa, H.2    Minagawa, T.3
  • 26
    • 0019180326 scopus 로고
    • Murein transglycosylase from phage lambda lysate. Purification and properties
    • Bienkowska-Szewczyk K, Taylor A, (1980) Murein transglycosylase from phage lambda lysate. Purification and properties. Biochim Biophys Acta 615: 489-496.
    • (1980) Biochim Biophys Acta , vol.615 , pp. 489-496
    • Bienkowska-Szewczyk, K.1    Taylor, A.2
  • 27
    • 0342655941 scopus 로고    scopus 로고
    • The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli
    • Kedzierska S, Wawrzynow A, Taylor A, (1996) The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli. Gene 168: 1-8.
    • (1996) Gene , vol.168 , pp. 1-8
    • Kedzierska, S.1    Wawrzynow, A.2    Taylor, A.3
  • 28
    • 0030045605 scopus 로고    scopus 로고
    • A protein linkage map of Escherichia coli bacteriophage T7
    • Bartel PL, Roecklein JA, SenGupta D, Fields S, (1996) A protein linkage map of Escherichia coli bacteriophage T7. Nat Genet 12: 72-77.
    • (1996) Nat Genet , vol.12 , pp. 72-77
    • Bartel, P.L.1    Roecklein, J.A.2    SenGupta, D.3    Fields, S.4
  • 29
    • 52649112247 scopus 로고    scopus 로고
    • The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes
    • Berry J, Summer EJ, Struck DK, Young R, (2008) The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes. Mol Microbiol 70: 341-351.
    • (2008) Mol Microbiol , vol.70 , pp. 341-351
    • Berry, J.1    Summer, E.J.2    Struck, D.K.3    Young, R.4
  • 30
    • 24944579983 scopus 로고    scopus 로고
    • Changes in bacteriophage T7 virion structure at the initiation of infection
    • Kemp P, Garcia LR, Molineux IJ, (2005) Changes in bacteriophage T7 virion structure at the initiation of infection. Virology 340: 307-317.
    • (2005) Virology , vol.340 , pp. 307-317
    • Kemp, P.1    Garcia, L.R.2    Molineux, I.J.3
  • 31
    • 0015834606 scopus 로고
    • DNA base sequence homology between coliphages T7 and phiII and between T3 and phiII as determined by heteroduplex mapping in the electron microscope
    • Hyman RW, Brunovskis I, Summers WC, (1973) DNA base sequence homology between coliphages T7 and phiII and between T3 and phiII as determined by heteroduplex mapping in the electron microscope. J Mol Biol 77: 189-196.
    • (1973) J Mol Biol , vol.77 , pp. 189-196
    • Hyman, R.W.1    Brunovskis, I.2    Summers, W.C.3
  • 32
    • 0021849311 scopus 로고
    • Isolation and characterization of bacteriophage T3/T7 hybrids and their use in studies on molecular basis of DNA-packaging specificity
    • Yamagishi M, Fujisawa H, Minagawa T, (1985) Isolation and characterization of bacteriophage T3/T7 hybrids and their use in studies on molecular basis of DNA-packaging specificity. Virology 144: 502-515.
    • (1985) Virology , vol.144 , pp. 502-515
    • Yamagishi, M.1    Fujisawa, H.2    Minagawa, T.3
  • 33
    • 0029008516 scopus 로고
    • Isolation of transcriptionally active mutants of T7 RNA polymerase that do not support phage growth
    • Zhang X, Studier FW, (1995) Isolation of transcriptionally active mutants of T7 RNA polymerase that do not support phage growth. J Mol Biol 250: 156-168.
    • (1995) J Mol Biol , vol.250 , pp. 156-168
    • Zhang, X.1    Studier, F.W.2
  • 34
    • 3042558419 scopus 로고    scopus 로고
    • Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection
    • Zhang X, Studier FW, (2004) Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection. J Mol Biol 340: 707-730.
    • (2004) J Mol Biol , vol.340 , pp. 707-730
    • Zhang, X.1    Studier, F.W.2
  • 35
    • 0029145564 scopus 로고
    • Analysis of the fine structure of the prohead binding domain of the packaging protein of bacteriophage T3 using a hexapeptide, an analog of a prohead binding site
    • Morita M, Tasaka M, Fujisawa H, (1995) Analysis of the fine structure of the prohead binding domain of the packaging protein of bacteriophage T3 using a hexapeptide, an analog of a prohead binding site. Virology 211: 516-524.
    • (1995) Virology , vol.211 , pp. 516-524
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 36
    • 33745179890 scopus 로고    scopus 로고
    • Structural recognition between a four-way DNA junction and a resolving enzyme
    • Declais AC, Liu J, Freeman AD, Lilley DM, (2006) Structural recognition between a four-way DNA junction and a resolving enzyme. J Mol Biol 359: 1261-1276.
    • (2006) J Mol Biol , vol.359 , pp. 1261-1276
    • Declais, A.C.1    Liu, J.2    Freeman, A.D.3    Lilley, D.M.4
  • 37
    • 0025850530 scopus 로고
    • Resolution of branched DNA substrates by T7 endonuclease I and its inhibition
    • Lu M, Guo Q, Studier FW, Kallenbach NR, (1991) Resolution of branched DNA substrates by T7 endonuclease I and its inhibition. J Biol Chem 266: 2531-2536.
    • (1991) J Biol Chem , vol.266 , pp. 2531-2536
    • Lu, M.1    Guo, Q.2    Studier, F.W.3    Kallenbach, N.R.4
  • 38
    • 0029933249 scopus 로고    scopus 로고
    • Single-stranded DNA binding protein and DNA helicase of bacteriophage T7 mediate homologous DNA strand exchange
    • Kong D, Richardson CC, (1996) Single-stranded DNA binding protein and DNA helicase of bacteriophage T7 mediate homologous DNA strand exchange. Embo J 15: 2010-2019.
    • (1996) Embo J , vol.15 , pp. 2010-2019
    • Kong, D.1    Richardson, C.C.2
  • 39
    • 0015499976 scopus 로고
    • Gene 6 exonuclease of bacteriophage T7. II. Mechanism of the reaction
    • Kerr C, Sadowski PD, (1972) Gene 6 exonuclease of bacteriophage T7. II. Mechanism of the reaction. J Biol Chem 247: 311-318.
    • (1972) J Biol Chem , vol.247 , pp. 311-318
    • Kerr, C.1    Sadowski, P.D.2
  • 40
    • 0021112574 scopus 로고
    • Bacteriophage T7 DNA replication. Synthesis of lagging strands in a reconstituted system using purified proteins
    • Engler MJ, Richardson CC, (1983) Bacteriophage T7 DNA replication. Synthesis of lagging strands in a reconstituted system using purified proteins. J Biol Chem 258: 11197-11205.
    • (1983) J Biol Chem , vol.258 , pp. 11197-11205
    • Engler, M.J.1    Richardson, C.C.2
  • 41
    • 0015499993 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3′ leads to 5′ exonuclease activity in deoxyribonucleic acid polymerases
    • Brutlag D, Kornberg A, (1972) Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3′ leads to 5′ exonuclease activity in deoxyribonucleic acid polymerases. J Biol Chem 247: 241-248.
    • (1972) J Biol Chem , vol.247 , pp. 241-248
    • Brutlag, D.1    Kornberg, A.2
  • 42
    • 1942488227 scopus 로고    scopus 로고
    • Characterization of bacteriophage T3 DNA ligase
    • Cai L, Hu C, Shen S, Wang W, Huang W, (2004) Characterization of bacteriophage T3 DNA ligase. J Biochem 135: 397-403.
    • (2004) J Biochem , vol.135 , pp. 397-403
    • Cai, L.1    Hu, C.2    Shen, S.3    Wang, W.4    Huang, W.5
  • 44
    • 0022689021 scopus 로고
    • Homologous recombination in Escherichia coli: dependence on substrate length and homology
    • Shen P, Huang HV, (1986) Homologous recombination in Escherichia coli: dependence on substrate length and homology. Genetics 112: 441-457.
    • (1986) Genetics , vol.112 , pp. 441-457
    • Shen, P.1    Huang, H.V.2
  • 45
    • 0000332222 scopus 로고
    • Evolution of dsDNA tailed-bacteriophage genomes
    • Casjens S, Hatfull G, Hendrix R, (1992) Evolution of dsDNA tailed-bacteriophage genomes. Semin Virol 3: 383-397.
    • (1992) Semin Virol , vol.3 , pp. 383-397
    • Casjens, S.1    Hatfull, G.2    Hendrix, R.3
  • 46
    • 0021361435 scopus 로고
    • Characterization of the cloned fip gene and its product
    • Russel M, Model P, (1984) Characterization of the cloned fip gene and its product. J Bacteriol 157: 526-532.
    • (1984) J Bacteriol , vol.157 , pp. 526-532
    • Russel, M.1    Model, P.2
  • 47
    • 0021256117 scopus 로고
    • Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12
    • Lunn CA, Kathju S, Wallace BJ, Kushner SR, Pigiet V, (1984) Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12. J Biol Chem 259: 10469-10474.
    • (1984) J Biol Chem , vol.259 , pp. 10469-10474
    • Lunn, C.A.1    Kathju, S.2    Wallace, B.J.3    Kushner, S.R.4    Pigiet, V.5
  • 48
    • 0942301389 scopus 로고    scopus 로고
    • A positive charge at position 33 of thioredoxin primarily affects its interaction with other proteins but not redox potential
    • Lin TY, Chen TS, (2004) A positive charge at position 33 of thioredoxin primarily affects its interaction with other proteins but not redox potential. Biochemistry 43: 945-952.
    • (2004) Biochemistry , vol.43 , pp. 945-952
    • Lin, T.Y.1    Chen, T.S.2
  • 49
    • 0015177611 scopus 로고
    • Effect of polymyxin on the bacteriophage receptors of the cell walls of gram-negative bacteria
    • Koike M, Iida K, (1971) Effect of polymyxin on the bacteriophage receptors of the cell walls of gram-negative bacteria. J Bacteriol 108: 1402-1411.
    • (1971) J Bacteriol , vol.108 , pp. 1402-1411
    • Koike, M.1    Iida, K.2
  • 50
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European Molecular Biology Open Software Suite
    • Rice P, Longden I, Bleasby A, (2000) EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet 16: 276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.