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Volumn 185, Issue 8, 2003, Pages 2465-2474

Bacteriophage SPP1 Chu is an alkaline exonuclease in the SynExo family of viral two-component recombinases

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; DOUBLE STRANDED DNA; EXONUCLEASE; OLIGOMER; RECOMBINASE;

EID: 0037389423     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.8.2465-2474.2003     Document Type: Article
Times cited : (42)

References (51)
  • 1
    • 0344863179 scopus 로고    scopus 로고
    • The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1
    • Alonso, J. C., G. Lüder, A. C. Stiege, S. Chai, F. Weise, and T. A. Trautner. 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    Lüder, G.2    Stiege, A.C.3    Chai, S.4    Weise, F.5    Trautner, T.A.6
  • 3
    • 0034664813 scopus 로고    scopus 로고
    • Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind, L., K. S. Makarova, and E. V. Koonin. 2000. Holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res. 28:3417-3432.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 4
    • 0037184023 scopus 로고    scopus 로고
    • Homologous-pairing activity of the Bacillus subtilis bacteriophage SPP1 replication protein G35P
    • Ayora, S., R. Missich, P. Mesa, R. Lurz, S. Yang, E. H. Egelman, and J. C. Alonso. 2002. Homologous-pairing activity of the Bacillus subtilis bacteriophage SPP1 replication protein G35P. J. Biol. Chem. 277:35969-35979.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35969-35979
    • Ayora, S.1    Missich, R.2    Mesa, P.3    Lurz, R.4    Yang, S.5    Egelman, E.H.6    Alonso, J.C.7
  • 6
    • 0015239451 scopus 로고
    • The role of exonuclease and beta protein of phage lambda in genetic recombination. II. Substrate specificity and the mode of action of lambda exonuclease
    • Carter, D. M., and C. M. Radding. 1971. The role of exonuclease and beta protein of phage lambda in genetic recombination. II. Substrate specificity and the mode of action of lambda exonuclease. J. Biol. Chem. 246:2502-2512.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2502-2512
    • Carter, D.M.1    Radding, C.M.2
  • 7
    • 0029129145 scopus 로고
    • Virus DNA packaging: The strategy used by phage lambda
    • Catalano, C. E., D. Cue, and M. Feiss. 1995. Virus DNA packaging: the strategy used by phage lambda. Mol. Microbiol. 16:1075-1086.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 8
    • 0035824602 scopus 로고    scopus 로고
    • Structure and function of the Escherichia coli RecE protein, a member of the RecB nuclease domain family
    • Chang, H. W., and D. A. Julin. 2001. Structure and function of the Escherichia coli RecE protein, a member of the RecB nuclease domain family. J. Biol. Chem. 276:46004-46010.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46004-46010
    • Chang, H.W.1    Julin, D.A.2
  • 9
    • 0035487293 scopus 로고    scopus 로고
    • Recombineering: A powerful new tool for mouse functional genomics
    • Copeland, N. G., N. A. Jenkins, and D. L. Court. 2001. Recombineering: a powerful new tool for mouse functional genomics. Nat. Rev. Genet. 2:769-779.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 769-779
    • Copeland, N.G.1    Jenkins, N.A.2    Court, D.L.3
  • 10
    • 0035810938 scopus 로고    scopus 로고
    • High efficiency mutagenesis, repair, and engineering of chromosomal DNA using single-stranded oligonucleotides
    • Ellis, H. M., D. Yu, T. DiTizio, and D. L. Court. 2001. High efficiency mutagenesis, repair, and engineering of chromosomal DNA using single-stranded oligonucleotides. Proc. Natl. Acad. Sci. USA 98: 6742-6746.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6742-6746
    • Ellis, H.M.1    Yu, D.2    DiTizio, T.3    Court, D.L.4
  • 11
    • 0018383288 scopus 로고
    • Packaging of the bacteriophage lambda chromosome: Dependence of cos cleavage on chromosome length
    • Feiss, M., and D. A. Siegele. 1979. Packaging of the bacteriophage lambda chromosome: dependence of cos cleavage on chromosome length. Virology 92:190-200.
    • (1979) Virology , vol.92 , pp. 190-200
    • Feiss, M.1    Siegele, D.A.2
  • 12
    • 0019421485 scopus 로고
    • Genetic analysis of the RecE pathway of genetic recombination in Escherichia coli K-12
    • Gillen, J. R., D. K. Willis, and A. J. Clark. 1981. Genetic analysis of the RecE pathway of genetic recombination in Escherichia coli K-12. J. Bacteriol. 145:521-532.
    • (1981) J. Bacteriol. , vol.145 , pp. 521-532
    • Gillen, J.R.1    Willis, D.K.2    Clark, A.J.3
  • 13
    • 0032503242 scopus 로고    scopus 로고
    • The exonuclease activity of HSV-1 UL12 is required for in vivo function
    • Goldstein, J. N., and S. K. Weller. 1998. The exonuclease activity of HSV-1 UL12 is required for in vivo function. Virology 244:442-457.
    • (1998) Virology , vol.244 , pp. 442-457
    • Goldstein, J.N.1    Weller, S.K.2
  • 14
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • Hanahan, D., J. Jessee, and F. R. Bloom. 1991, Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol. 204:63-113.
    • (1991) Methods Enzymol. , vol.204 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 17
    • 0031006470 scopus 로고    scopus 로고
    • Single-strand DNA intermediates in phage lambda's Red recombination pathway
    • Hill, S. A., M. M. Stahl, and F. W. Stahl. 1997. Single-strand DNA intermediates in phage lambda's Red recombination pathway. Proc. Natl. Acad. Sci. USA 94:2951-2956.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2951-2956
    • Hill, S.A.1    Stahl, M.M.2    Stahl, F.W.3
  • 19
    • 9144244444 scopus 로고    scopus 로고
    • Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52
    • Iyer, L. M., E. V. Koonin, and L. Aravind. 2002. Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52. BMC Genomics 3:8-18.
    • (2002) BMC Genomics , vol.3 , pp. 8-18
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 20
    • 0018721473 scopus 로고
    • Physical characterisation of the "Rac prophage" in E. coli K12
    • Kaiser, K., and N. E. Murray. 1979. Physical characterisation of the "Rac prophage" in E. coli K12. Mol. Gen. Genet. 175:159-174.
    • (1979) Mol. Gen. Genet. , vol.175 , pp. 159-174
    • Kaiser, K.1    Murray, N.E.2
  • 21
    • 0030881051 scopus 로고    scopus 로고
    • Toroidal structure of lambda-exonuclease
    • Kovall, R., and B. W. Mathews. 1997. Toroidal structure of lambda-exonuclease. Science 277:1824-1827.
    • (1997) Science , vol.277 , pp. 1824-1827
    • Kovall, R.1    Mathews, B.W.2
  • 22
    • 0028224075 scopus 로고
    • Involvement of RecE exonuclease and RecT annealing protein in DNA double-strand break repair by homologous recombination
    • Kusano, K., N. K. Takahashi, H. Yoshikura, and I. Kobayashi. 1994. Involvement of RecE exonuclease and RecT annealing protein in DNA double-strand break repair by homologous recombination. Gene 138:17-25.
    • (1994) Gene , vol.138 , pp. 17-25
    • Kusano, K.1    Takahashi, N.K.2    Yoshikura, H.3    Kobayashi, I.4
  • 23
    • 0032489359 scopus 로고    scopus 로고
    • The beta protein of phage lambda promotes strand exchange
    • Li, Z., G. Karakousis, S. K. Chiu, G. Reddy, and C. M. Radding. 1998. The beta protein of phage lambda promotes strand exchange. J. Mol. Biol. 276: 733-744.
    • (1998) J. Mol. Biol. , vol.276 , pp. 733-744
    • Li, Z.1    Karakousis, G.2    Chiu, S.K.3    Reddy, G.4    Radding, C.M.5
  • 24
    • 0014216084 scopus 로고
    • An exonuclease induced by bacteriophage lambda. II. Nature of the enzymatic reaction
    • Little, J. W. 1967. An exonuclease induced by bacteriophage lambda. II. Nature of the enzymatic reaction. J. Biol. Chem. 242:679-686.
    • (1967) J. Biol. Chem. , vol.242 , pp. 679-686
    • Little, J.W.1
  • 25
    • 0014216121 scopus 로고
    • An exonuclease induced by bacteriophage lambda. I. Preparation of the crystalline enzyme
    • Little, J. W., I. R. Lehman, and A. D. Kaiser. 1967. An exonuclease induced by bacteriophage lambda. I. Preparation of the crystalline enzyme. J. Biol. Chem. 242:672-678.
    • (1967) J. Biol. Chem. , vol.242 , pp. 672-678
    • Little, J.W.1    Lehman, I.R.2    Kaiser, A.D.3
  • 27
    • 0033178687 scopus 로고    scopus 로고
    • Characterization of the interaction of lambda exonuclease with the ends of DNA
    • Mitsis, P. G., and J. G. Kwagh. 1999. Characterization of the interaction of lambda exonuclease with the ends of DNA. Nucleic Acids Res. 27:3057-3063.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3057-3063
    • Mitsis, P.G.1    Kwagh, J.G.2
  • 28
    • 0022912797 scopus 로고
    • The homologous recombination system of phage lambda. Pairing activities of beta protein
    • Muniyappa, K., and C. M. Radding. 1986. The homologous recombination system of phage lambda. Pairing activities of beta protein. J. Biol. Chem. 261:7472-7478.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7472-7478
    • Muniyappa, K.1    Radding, C.M.2
  • 29
    • 0033624563 scopus 로고    scopus 로고
    • RecE/RecT and Redα/Redβ initiate double-stranded break repair by specifically interacting with their respective partners
    • Muyrers, J. P., Y. Zhang, F. Buchholz, and A. F. Stewart. 2000. RecE/RecT and Redα/Redβ initiate double-stranded break repair by specifically interacting with their respective partners. Genes Dev. 14:1971-1982.
    • (2000) Genes Dev. , vol.14 , pp. 1971-1982
    • Muyrers, J.P.1    Zhang, Y.2    Buchholz, F.3    Stewart, A.F.4
  • 30
    • 0002748070 scopus 로고    scopus 로고
    • Mining DNA sequences for molecular enzymology: The Redα superfamily defines a set of recombination nucleases
    • Oxford University Press, Oxford, United Kingdom
    • Myers, R. S., and K. E. Rudd. 1998. Mining DNA sequences for molecular enzymology: the Redα superfamily defines a set of recombination nucleases, p. 49-50. In Proceedings of the 1998 Miami Nature Biotechnology Winter Symposium. Oxford University Press, Oxford, United Kingdom.
    • (1998) Proceedings of the 1998 Miami Nature Biotechnology Winter Symposium , pp. 49-50
    • Myers, R.S.1    Rudd, K.E.2
  • 31
    • 0032524617 scopus 로고    scopus 로고
    • DNA strand invasion promoted by Escherichia coli RecT protein
    • Noirot, P., and R. D. Kolodner. 1998. DNA strand invasion promoted by Escherichia coli RecT protein. J. Biol. Chem. 273:12274-12280.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12274-12280
    • Noirot, P.1    Kolodner, R.D.2
  • 32
    • 0033551177 scopus 로고    scopus 로고
    • Rings and filaments of beta protein from bacteriophage lambda suggest a superfamily of recombination proteins
    • Passy, S. I., X. Yu, Z. Li, C. M. Radding, and E. H. Egelman. 1999. Rings and filaments of beta protein from bacteriophage lambda suggest a superfamily of recombination proteins. Proc. Natl. Acad. Sci. USA 96:4279-4284.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4279-4284
    • Passy, S.I.1    Yu, X.2    Li, Z.3    Radding, C.M.4    Egelman, E.H.5
  • 33
    • 0013924499 scopus 로고
    • Regulation of lambda exonuclease. I. Properties of lambda exonuclease purified from lysogens of lambda T11 and wild type
    • Radding, C. M. 1966. Regulation of lambda exonuclease. I. Properties of lambda exonuclease purified from lysogens of lambda T11 and wild type. J. Mol. Biol. 18:235-250.
    • (1966) J. Mol. Biol. , vol.18 , pp. 235-250
    • Radding, C.M.1
  • 35
    • 0344374737 scopus 로고
    • Origin of DNA concatemers during growth
    • A. D. Hershey (ed.). Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Skalka, A. 1971. Origin of DNA concatemers during growth, p. 535-547. In A. D. Hershey (ed.), The bacteriophage lambda. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1971) The Bacteriophage Lambda , pp. 535-547
    • Skalka, A.1
  • 36
    • 0000802462 scopus 로고
    • General recombination
    • R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.). Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Smith, G. R. 1983. General recombination, p. 175-209. In R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Lambda II. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1983) Lambda II , pp. 175-209
    • Smith, G.R.1
  • 38
    • 0015457788 scopus 로고
    • An enhancing role for DNA synthesis in formation of bacteriophage lambda recombinants
    • Stahl, F. W., K. D. McMilin, M. M. Stahl, and Y. Nozu. 1972. An enhancing role for DNA synthesis in formation of bacteriophage lambda recombinants. Proc. Natl. Acad. Sci. USA 69:3598-3601.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3598-3601
    • Stahl, F.W.1    McMilin, K.D.2    Stahl, M.M.3    Nozu, Y.4
  • 40
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 41
    • 0025357164 scopus 로고
    • Evidence for the double-strand break repair model of bacteriophage lambda recombination
    • Takahashi, N., and I. Kobayashi. 1990. Evidence for the double-strand break repair model of bacteriophage lambda recombination. Proc. Natf. Acad. Sci. USA 87:2790-2794.
    • (1990) Proc. Natf. Acad. Sci. USA , vol.87 , pp. 2790-2794
    • Takahashi, N.1    Kobayashi, I.2
  • 42
    • 0030596178 scopus 로고    scopus 로고
    • Sequential headful packaging and fate of the cleaved DNA ends in bacteriophage SPP1
    • Tavares, P., R. Lurz, A. Stiege, B. Rückert, and T. A. Trautner. 1996. Sequential headful packaging and fate of the cleaved DNA ends in bacteriophage SPP1. J. Mol. Biol. 264:954-967.
    • (1996) J. Mol. Biol. , vol.264 , pp. 954-967
    • Tavares, P.1    Lurz, R.2    Stiege, A.3    Rückert, B.4    Trautner, T.A.5
  • 43
    • 0023644769 scopus 로고
    • Double-chain-cut sites are recombination hotspots in the Red pathway of phage lambda
    • Thaler, D. S., M. M. Stahl, and F. W. Stahl. 1987. Double-chain-cut sites are recombination hotspots in the Red pathway of phage lambda. J. Mol. Biol. 195:75-87.
    • (1987) J. Mol. Biol. , vol.195 , pp. 75-87
    • Thaler, D.S.1    Stahl, M.M.2    Stahl, F.W.3
  • 44
    • 0026540993 scopus 로고
    • Association between the herpes simplex virus major DNA-binding protein and alkaline nuclease
    • Thomas, M. S., M. Gao, D. M. Knipe, and K. L. Powell. 1992. Association between the herpes simplex virus major DNA-binding protein and alkaline nuclease. J. Virol. 66:1152-1161.
    • (1992) J. Virol. , vol.66 , pp. 1152-1161
    • Thomas, M.S.1    Gao, M.2    Knipe, D.M.3    Powell, K.L.4
  • 45
    • 0031582078 scopus 로고    scopus 로고
    • In vivo packaging of bacteriophage lambda monomeric chromosomes
    • Thomason, L. C., D. S. Thaler, M. M. Stahl, and F. W. Stahl. 1997. In vivo packaging of bacteriophage lambda monomeric chromosomes. J. Mol. Biol. 267:75-87.
    • (1997) J. Mol. Biol. , vol.267 , pp. 75-87
    • Thomason, L.C.1    Thaler, D.S.2    Stahl, M.M.3    Stahl, F.W.4
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompsom J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompsom, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0020327471 scopus 로고
    • Site-specific cleavage/packaging of herpes simplex virus DNA and the selective maturation of nucleocapsids containing full-length viral DNA
    • Vlazny, D. A., A. Kwong, and N. Frenkel. 1982. Site-specific cleavage/packaging of herpes simplex virus DNA and the selective maturation of nucleocapsids containing full-length viral DNA. Proc. Natl. Acad. Sci. USA 79: 1423-1427.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1423-1427
    • Vlazny, D.A.1    Kwong, A.2    Frenkel, N.3
  • 49
    • 0027968224 scopus 로고
    • Nucleoticle sequence and complementation studies of the gene 35 region of the Bacillus subtilis bacteriophage SPP1
    • Wiese, F., S. Chai, G. Lüder, and J. C. Alonso. 1994 Nucleoticle sequence and complementation studies of the gene 35 region of the Bacillus subtilis bacteriophage SPP1. Virology 202:1046-1049.
    • (1994) Virology , vol.202 , pp. 1046-1049
    • Wiese, F.1    Chai, S.2    Lüder, G.3    Alonso, J.C.4
  • 50
    • 0033064965 scopus 로고    scopus 로고
    • Replication, integration, and packaging of plasmid DNA following cotransfection with baculovirus viral DNA
    • Wu, Y., G. Liu, and E. B. Carstens. 1999. Replication, integration, and packaging of plasmid DNA following cotransfection with baculovirus viral DNA. J. Virol. 73:5473-5480.
    • (1999) J. Virol. , vol.73 , pp. 5473-5480
    • Wu, Y.1    Liu, G.2    Carstens, E.B.3
  • 51
    • 0028859088 scopus 로고
    • Evidence for conservative (two-progeny) DNA double-strand break repair
    • Yokochi, T., K. Kusano, and I. Kobayashi. 1995. Evidence for conservative (two-progeny) DNA double-strand break repair. Genetics 139:5-17.
    • (1995) Genetics , vol.139 , pp. 5-17
    • Yokochi, T.1    Kusano, K.2    Kobayashi, I.3


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