메뉴 건너뛰기




Volumn 61, Issue , 2007, Pages 1-22

40 Years with bacteriophage ø29

Author keywords

DNA polymerase; Protein priming; Replication; Terminal protein; Transcription

Indexed keywords

DNA POLYMERASE; VIRUS PROTEIN;

EID: 35848953218     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.61.080706.093415     Document Type: Review
Times cited : (10)

References (47)
  • 1
    • 0013909852 scopus 로고
    • Structure of Bacillus subtilis bacteriophage ø29 and the length of ø29 deoxyribonucleic acid
    • Anderson DL, Hickman DD, Reilly BE. 1966. Structure of Bacillus subtilis bacteriophage ø29 and the length of ø29 deoxyribonucleic acid. J. Bacteriol. 91:2081-89
    • (1966) J. Bacteriol , vol.91 , pp. 2081-2089
    • Anderson, D.L.1    Hickman, D.D.2    Reilly, B.E.3
  • 2
    • 0014964703 scopus 로고
    • Subunit composition of B. subtilis RNA polymerase
    • Avila J, Hermoso JM, Viñuela E, Salas M. 1970. Subunit composition of B. subtilis RNA polymerase. Nature 226:1244-45
    • (1970) Nature , vol.226 , pp. 1244-1245
    • Avila, J.1    Hermoso, J.M.2    Viñuela, E.3    Salas, M.4
  • 3
    • 33646077199 scopus 로고    scopus 로고
    • The structure of ø29 transcription regulator p4-DNA complex reveals a novel DNA binding motif
    • Badía D, Camacho A, Pérez-Lago L, Escandón C, Salas M, Coll M. 2006. The structure of ø29 transcription regulator p4-DNA complex reveals a novel DNA binding motif. Mol. Cell 22:73-81
    • (2006) Mol. Cell , vol.22 , pp. 73-81
    • Badía, D.1    Camacho, A.2    Pérez-Lago, L.3    Escandón, C.4    Salas, M.5    Coll, M.6
  • 4
    • 0024474078 scopus 로고
    • A conserved 3′-5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases
    • Bernad A, Blanco L, Lázaro JM, Martín G, Salas M. 1989. A conserved 3′-5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases. Cell 59:219-28
    • (1989) Cell , vol.59 , pp. 219-228
    • Bernad, A.1    Blanco, L.2    Lázaro, J.M.3    Martín, G.4    Salas, M.5
  • 5
    • 0024335104 scopus 로고
    • Highly efficient DNA synthesis by the phage ø29 DNA polymerase. Symmetrical mode of DNA replication
    • Blanco L, Bernad A, Lázaro JM, Martín G, Garmendia C, Salas M. 1989. Highly efficient DNA synthesis by the phage ø29 DNA polymerase. Symmetrical mode of DNA replication. J. Biol. Chem. 264:8935-40
    • (1989) J. Biol. Chem , vol.264 , pp. 8935-8940
    • Blanco, L.1    Bernad, A.2    Lázaro, J.M.3    Martín, G.4    Garmendia, C.5    Salas, M.6
  • 7
    • 0009749157 scopus 로고
    • Replication of ø29 DNA with purified terminal protein and DNA polymerase: Synthesis of full-length ø29 DNA
    • Blanco L, Salas M. 1985. Replication of ø29 DNA with purified terminal protein and DNA polymerase: synthesis of full-length ø29 DNA. Proc. Natl. Acad. Sci. USA 82:6404-8
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6404-6408
    • Blanco, L.1    Salas, M.2
  • 8
    • 0029879312 scopus 로고    scopus 로고
    • Relating structure to function in ø29 DNA polymerase
    • Blanco L, Salas M. 1996. Relating structure to function in ø29 DNA polymerase. J. Biol. Chem. 271:8509-12
    • (1996) J. Biol. Chem , vol.271 , pp. 8509-8512
    • Blanco, L.1    Salas, M.2
  • 10
    • 0034830935 scopus 로고    scopus 로고
    • Rapid amplification of plasmid and phage DNA using ø29 DNA polymerase and multiply-primed rolling circle amplification
    • Dean FB, Nelson JR, Geisler TL, Lasken RS. 2001. Rapid amplification of plasmid and phage DNA using ø29 DNA polymerase and multiply-primed rolling circle amplification. Genome Res. 11:1095-99
    • (2001) Genome Res , vol.11 , pp. 1095-1099
    • Dean, F.B.1    Nelson, J.R.2    Geisler, T.L.3    Lasken, R.S.4
  • 11
    • 0039554345 scopus 로고    scopus 로고
    • Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of ø29 early-late transcriptional switch
    • Elías-Arnanz M, Salas M. 1999. Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of ø29 early-late transcriptional switch. Genes Dev. 13:2502-13
    • (1999) Genes Dev , vol.13 , pp. 2502-2513
    • Elías-Arnanz, M.1    Salas, M.2
  • 12
    • 0001719080 scopus 로고
    • Enzymatic synthesis and breakdown of polynucleotides; polynucleotide Phosphorylase
    • Grunberg-Manago M, Ochoa S. 1955. Enzymatic synthesis and breakdown of polynucleotides; polynucleotide Phosphorylase. J. Am. Chem. Soc. 77:3165-66
    • (1955) J. Am. Chem. Soc , vol.77 , pp. 3165-3166
    • Grunberg-Manago, M.1    Ochoa, S.2
  • 13
    • 0023225629 scopus 로고    scopus 로고
    • 198 7. A small viral RNA is required for in vitro packaging of bacteriophage ø29 DNA
    • Guo P, Erickson S, Anderson D. 198 7. A small viral RNA is required for in vitro packaging of bacteriophage ø29 DNA. Science 236:690-94
    • Science , vol.236 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 14
    • 8844274078 scopus 로고    scopus 로고
    • Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage ø29
    • Kamtekar S, Berman A, Wang J, Lazaro JM, de Vega M, et al. 2004. Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage ø29. Mol. Cell 16:609-18
    • (2004) Mol. Cell , vol.16 , pp. 609-618
    • Kamtekar, S.1    Berman, A.2    Wang, J.3    Lazaro, J.M.4    de Vega, M.5
  • 15
    • 33645303495 scopus 로고    scopus 로고
    • Structure of bacteriophage ø29 DNA polymerase bound to its protein-primer: Implications for the transition from initiation to elongation
    • Kamtekar S, Berman A, Wang J, Lazaro JM, de Vega M, et al. 2006. Structure of bacteriophage ø29 DNA polymerase bound to its protein-primer: implications for the transition from initiation to elongation. EMBO J. 25:1335-43
    • (2006) EMBO J , vol.25 , pp. 1335-1343
    • Kamtekar, S.1    Berman, A.2    Wang, J.3    Lazaro, J.M.4    de Vega, M.5
  • 17
    • 27144556385 scopus 로고    scopus 로고
    • Molecular basis for the exploitation of spore formation as survival mechanism by virulent phage phi29
    • Meijer WJ, Castilla-Llorente V, Villar L, Murray H, Errington J, Salas M. 2005. Molecular basis for the exploitation of spore formation as survival mechanism by virulent phage phi29. EMBO J. 24:3647-57
    • (2005) EMBO J , vol.24 , pp. 3647-3657
    • Meijer, W.J.1    Castilla-Llorente, V.2    Villar, L.3    Murray, H.4    Errington, J.5    Salas, M.6
  • 18
    • 0017178260 scopus 로고
    • Genetic analysis of bacteriophage ø29 of B. subtilis: Integration and mapping of reference mutants of two collections
    • Mellado RP, Moreno F, Viñuela E, Salas M, Reilly BE, Anderson DL. 1976. Genetic analysis of bacteriophage ø29 of B. subtilis: integration and mapping of reference mutants of two collections. J. Virol. 19:495-500
    • (1976) J. Virol , vol.19 , pp. 495-500
    • Mellado, R.P.1    Moreno, F.2    Viñuela, E.3    Salas, M.4    Reilly, B.E.5    Anderson, D.L.6
  • 19
    • 0026756601 scopus 로고
    • Initiation of ø29 DNA replication occurs at the second 3′ nucleotide of the linear template: A sliding-back mechanism for protein-primed DNA replication
    • Méndez J, Blanco L, Esteban JA, Bernad A, Salas M. 1992. Initiation of ø29 DNA replication occurs at the second 3′ nucleotide of the linear template: a sliding-back mechanism for protein-primed DNA replication. Proc. Natl. Acad Sci. USA 89:9579-83
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 9579-9583
    • Méndez, J.1    Blanco, L.2    Esteban, J.A.3    Bernad, A.4    Salas, M.5
  • 20
    • 0040528887 scopus 로고    scopus 로고
    • Protein-primed DNA replication: A transition between two modes of priming by a unique DNA polymerase
    • Méndez J, Blanco L, Salas M. 1997. Protein-primed DNA replication: a transition between two modes of priming by a unique DNA polymerase. EMBO J. 16:2519-27
    • (1997) EMBO J , vol.16 , pp. 2519-2527
    • Méndez, J.1    Blanco, L.2    Salas, M.3
  • 21
    • 0031300893 scopus 로고    scopus 로고
    • Transcription activation or repression by phage ø29 protein p4 depends on the strength of the RNA polymerase-promoter interactions
    • Monsalve M, Calles B, Mencía M, Salas M, Rojo F. 1997. Transcription activation or repression by phage ø29 protein p4 depends on the strength of the RNA polymerase-promoter interactions. Mol. Cell 1:1-9
    • (1997) Mol. Cell , vol.1 , pp. 1-9
    • Monsalve, M.1    Calles, B.2    Mencía, M.3    Salas, M.4    Rojo, F.5
  • 22
  • 23
    • 0343276268 scopus 로고
    • Initiation of phage ø29 DNA replication in vitro: Formation of a covalent complex between the terminal protein, p3, and 5′-dAMP
    • Peñalva MA, Salas M. 1982. Initiation of phage ø29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5′-dAMP. Proc. Natl. Acad. Sci. USA 79:5522-26
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5522-5526
    • Peñalva, M.A.1    Salas, M.2
  • 24
    • 0017736844 scopus 로고
    • Identification of a protein linked to the ends of adenovirus DNA
    • Rekosh DM, Russell WC, Bellet AJ, Robinson AJ. 1977. Identification of a protein linked to the ends of adenovirus DNA. Cell 11:283-95
    • (1977) Cell , vol.11 , pp. 283-295
    • Rekosh, D.M.1    Russell, W.C.2    Bellet, A.J.3    Robinson, A.J.4
  • 26
    • 18144365195 scopus 로고    scopus 로고
    • A specific subdomain in ø29 DNA polymerase confers both processivity and strand displacement capacity
    • Rodríguez I, Lázaro JM, Blanco L, Kamtekar S, Berman AJ, et al. 2005. A specific subdomain in ø29 DNA polymerase confers both processivity and strand displacement capacity. Proc. Natl. Acad. Sci. USA 102:6407-12
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6407-6412
    • Rodríguez, I.1    Lázaro, J.M.2    Blanco, L.3    Kamtekar, S.4    Berman, A.J.5
  • 27
    • 0031626930 scopus 로고    scopus 로고
    • Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase: The model of phage ø29 protein p4
    • Rojo F, Mencía M, Monsalve M, Salas M. 1998. Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase: the model of phage ø29 protein p4. Progr. Nucleic Acids Res. Mol. Biol. 60:29-46
    • (1998) Progr. Nucleic Acids Res. Mol. Biol , vol.60 , pp. 29-46
    • Rojo, F.1    Mencía, M.2    Monsalve, M.3    Salas, M.4
  • 28
    • 0001514043 scopus 로고
    • Glucokinase of rabbit liver: Purification and properties
    • Salas J, Salas M, Viñuela E, Sols A. 1965. Glucokinase of rabbit liver: purification and properties. J. Biol. Chem. 240:1014-18
    • (1965) J. Biol. Chem , vol.240 , pp. 1014-1018
    • Salas, J.1    Salas, M.2    Viñuela, E.3    Sols, A.4
  • 29
    • 34548554623 scopus 로고    scopus 로고
    • Bacteriophage protein-primed DNA replication
    • ed. KL Hefferon, pp, Kerala, India: Res. Signpost Transw. Res. Netw
    • Salas M, de Vega M. 2006. Bacteriophage protein-primed DNA replication. In Recent Advances in DNA Virus Replication, ed. KL Hefferon, pp. 259-88. Kerala, India: Res. Signpost Transw. Res. Netw.
    • (2006) Recent Advances in DNA Virus Replication , pp. 259-288
    • Salas, M.1    de Vega, M.2
  • 30
    • 35848968943 scopus 로고    scopus 로고
    • Salas M, de Vega M, Lázaro JM, Blanco L. 2004. ø29 DNA polymerase, a potent amplification enzyme. In DNA Amplification: Current Technologies and Applications, ed. VV Demidov, NE Broude, pp. 21-34. Norfolk, UK: Horizon Bioscience
    • Salas M, de Vega M, Lázaro JM, Blanco L. 2004. ø29 DNA polymerase, a potent amplification enzyme. In DNA Amplification: Current Technologies and Applications, ed. VV Demidov, NE Broude, pp. 21-34. Norfolk, UK: Horizon Bioscience
  • 31
    • 35848963684 scopus 로고
    • Translation of the genetic message. II. Effect of initiation factors on the binding of formyl-methionyl-tRNA to ribosomes
    • Salas M, Hille MB, Last JA, Wahba AJ, Ochoa S. 1967. Translation of the genetic message. II. Effect of initiation factors on the binding of formyl-methionyl-tRNA to ribosomes. Proc. Natl. Acad. Sci. USA 57:387-94
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 387-394
    • Salas, M.1    Hille, M.B.2    Last, J.A.3    Wahba, A.J.4    Ochoa, S.5
  • 32
    • 0017893449 scopus 로고
    • Characterization of a protein covalently linked to the 5′ termini of the DNA of Bacillus subtilis phage ø29
    • Salas M, Mellado RP, Viñuela E, Sogo JM. 1978. Characterization of a protein covalently linked to the 5′ termini of the DNA of Bacillus subtilis phage ø29. J. Mol. Biol. 119:269-91
    • (1978) J. Mol. Biol , vol.119 , pp. 269-291
    • Salas, M.1    Mellado, R.P.2    Viñuela, E.3    Sogo, J.M.4
  • 33
    • 0002277375 scopus 로고    scopus 로고
    • Mechanisms for priming DNA synthesis
    • ed. ML DePamphilis, pp, Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Salas M, Miller JT, Leis J, DePamphilis ML. 1996. Mechanisms for priming DNA synthesis. In DNA Replication in Eukaryotic Cells, ed. ML DePamphilis, pp. 131-76. Cold Spring Harbor, NY: Cold Spring Harbor Press
    • (1996) DNA Replication in Eukaryotic Cells , pp. 131-176
    • Salas, M.1    Miller, J.T.2    Leis, J.3    DePamphilis, M.L.4
  • 36
    • 0348112799 scopus 로고
    • Insulin-dependent synthesis of liver glucokinase in the rat
    • Salas M, Viñuela E, Sols A. 1963. Insulin-dependent synthesis of liver glucokinase in the rat. J. Biol. Chem. 238:3535-38
    • (1963) J. Biol. Chem , vol.238 , pp. 3535-3538
    • Salas, M.1    Viñuela, E.2    Sols, A.3
  • 37
    • 0000715089 scopus 로고
    • Spontaneous and enzymatically catalyzed anomerization of glucose-6-P and anomeric specificity of related enzymes
    • Salas M, Viñuela E, Sols A. 1965. Spontaneous and enzymatically catalyzed anomerization of glucose-6-P and anomeric specificity of related enzymes. J. Biol. Chem. 240:561-68
    • (1965) J. Biol. Chem , vol.240 , pp. 561-568
    • Salas, M.1    Viñuela, E.2    Sols, A.3
  • 39
    • 0025279627 scopus 로고
    • A novel nucleoprotein complex at a replication origin
    • Serrano M, Salas M, Hermoso JM. 1990. A novel nucleoprotein complex at a replication origin. Science 248:1012-16
    • (1990) Science , vol.248 , pp. 1012-1016
    • Serrano, M.1    Salas, M.2    Hermoso, J.M.3
  • 40
    • 33646360830 scopus 로고    scopus 로고
    • A uracil-DNA glycosylase inhibitor encoded by a non-uracil containing viral DNA
    • Serrano-Heras G, Salas M, Bravo A. 2006. A uracil-DNA glycosylase inhibitor encoded by a non-uracil containing viral DNA. J. Biol. Chem. 281:7068-74
    • (2006) J. Biol. Chem , vol.281 , pp. 7068-7074
    • Serrano-Heras, G.1    Salas, M.2    Bravo, A.3
  • 41
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro AL, Viñuela E, Maizel HV. 1967. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28:815-20
    • (1967) Biochem. Biophys. Res. Commun , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Viñuela, E.2    Maizel, H.V.3
  • 43
    • 0013927525 scopus 로고
    • Translation of the genetic message. I. Factors involved in the initiation of protein synthesis
    • Stanley WM Jr, Salas M, Wahba AJ, Ochoa S. 1966. Translation of the genetic message. I. Factors involved in the initiation of protein synthesis. Proc. Natl. Acad. Sci. USA 56:290-95
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 290-295
    • Stanley Jr, W.M.1    Salas, M.2    Wahba, A.J.3    Ochoa, S.4
  • 44
    • 0019522977 scopus 로고
    • Adsorption of bacteriophage ø29 to Bacillus subtilis through the neck appendages of the viral particle
    • Villanueva N, Salas M. 1981. Adsorption of bacteriophage ø29 to Bacillus subtilis through the neck appendages of the viral particle. J. Virol. 38:15-19
    • (1981) J. Virol , vol.38 , pp. 15-19
    • Villanueva, N.1    Salas, M.2
  • 45
    • 0014061191 scopus 로고
    • Synthesis of virus-specific proteins in E. coli infected with the RNA bacteriophage MS2
    • Viñuela E, Algranati MI, Ochoa S. 1967. Synthesis of virus-specific proteins in E. coli infected with the RNA bacteriophage MS2. Eur. J. Biochem. 1:3-11
    • (1967) Eur. J. Biochem , vol.1 , pp. 3-11
    • Viñuela, E.1    Algranati, M.I.2    Ochoa, S.3
  • 46
    • 35848960626 scopus 로고
    • Translation of the genetic message. III. Formylmethionine as initiator of proteins programed by polycistronic messenger RNA
    • Viñuela E, Salas M, Ochoa S. 1967. Translation of the genetic message. III. Formylmethionine as initiator of proteins programed by polycistronic messenger RNA. Proc. Natl. Acad. Sci. USA 57:729-34
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 729-734
    • Viñuela, E.1    Salas, M.2    Ochoa, S.3
  • 47
    • 0003226061 scopus 로고
    • Glucokinase and hexokinase in liver in relation to glycogen synthesis
    • Viñuela E, Salas M, Sols A. 1963. Glucokinase and hexokinase in liver in relation to glycogen synthesis. J. Biol. Chem. 238:1175-77
    • (1963) J. Biol. Chem , vol.238 , pp. 1175-1177
    • Viñuela, E.1    Salas, M.2    Sols, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.