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Volumn 32, Issue 11, 2004, Pages 3493-3502

Binding of phage φ29 architectural protein p6 to the viral genome: Evidence for topological restriction of the phage linear DNA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIOPHAGE DNA; CURVED DNA; DNA TOPOISOMERASE (ATP HYDROLYSING); NOVOBIOCIN; PROTEIN P6; UNCLASSIFIED DRUG; PHAGE PHI29 PROTEIN P6; VIRUS DNA; VIRUS PROTEIN;

EID: 4344592253     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh668     Document Type: Article
Times cited : (14)

References (69)
  • 3
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • Thomas,J.O. and Travers,A.A. (2001) HMG1 and 2, and related 'architectural' DNA-binding proteins. Trends Biochem. Sci., 26, 167-174.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 4
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: A role for HMGB proteins?
    • Travers,A.A. (2003) Priming the nucleosome: a role for HMGB proteins? EMBO Rep., 4, 131-136.
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, A.A.1
  • 5
    • 0032901198 scopus 로고    scopus 로고
    • SMC-mediated chromosome mechanics: A conserved scheme from bacteria to vertebrates?
    • Hirano,T. (1999) SMC-mediated chromosome mechanics: a conserved scheme from bacteria to vertebrates? Genes Dev., 13, 11-19.
    • (1999) Genes Dev. , vol.13 , pp. 11-19
    • Hirano, T.1
  • 6
    • 0033167929 scopus 로고    scopus 로고
    • Structural maintenance of chromosomes (SMC) proteins: Conserved molecular properties for multiple biological functions
    • Strunnikov,A.V. and Jessberger,R. (1999) Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions. Eur. J. Biochem., 263, 6-13.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 6-13
    • Strunnikov, A.V.1    Jessberger, R.2
  • 7
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica,K. and Rouvière-Yaniv,J. (1987) Histone-like proteins of bacteria. Microbiol. Rev., 51, 301-319.
    • (1987) Microbiol. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouvière-Yaniv, J.2
  • 8
    • 0029447826 scopus 로고
    • Nucleoid proteins
    • Hayat,M.A. and Mancarella,D.A. (1995) Nucleoid proteins. Micron, 26, 461-480.
    • (1995) Micron , vol.26 , pp. 461-480
    • Hayat, M.A.1    Mancarella, D.A.2
  • 9
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam,T.A., Iwata,A., Nishimura,A., Ueda,S. and Ishihama,A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol., 181, 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 10
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam,T.A., Hiraga,S. and Ishihama,A. (2000) Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes Cells, 5, 613-626.
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.A.1    Hiraga, S.2    Ishihama, A.3
  • 11
    • 0027097480 scopus 로고
    • E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities
    • Niki,H., Imamura,R., Kitaoka,M., Yamanaka,K., Ogura,T. and Hiraga,S. (1992) E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities. EMBO J., 11, 5101-5109.
    • (1992) EMBO J. , vol.11 , pp. 5101-5109
    • Niki, H.1    Imamura, R.2    Kitaoka, M.3    Yamanaka, K.4    Ogura, T.5    Hiraga, S.6
  • 12
    • 0030904358 scopus 로고    scopus 로고
    • Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis
    • Kohler,P. and Marahiel,M.A. (1997) Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis. J. Bacteriol., 179, 2060-2064.
    • (1997) J. Bacteriol. , vol.179 , pp. 2060-2064
    • Kohler, P.1    Marahiel, M.A.2
  • 13
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • Tapias,A., López,G. and Ayora,S. (2000) Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA. Nucleic Acids Res., 28, 552-559.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 552-559
    • Tapias, A.1    López, G.2    Ayora, S.3
  • 14
    • 0035085543 scopus 로고    scopus 로고
    • A possible role for L24 of Bacillus subtilis in nucleoid organization and segregation
    • Exley,R., Zouine,M., Pernelle,J.J., Beloin,C., Le Hegarat,F. and Deneubourg,A.M. (2001) A possible role for L24 of Bacillus subtilis in nucleoid organization and segregation. Biochimie, 83, 269-275.
    • (2001) Biochimie , vol.83 , pp. 269-275
    • Exley, R.1    Zouine, M.2    Pernelle, J.J.3    Beloin, C.4    Le Hegarat, F.5    Deneubourg, A.M.6
  • 15
    • 0035119398 scopus 로고    scopus 로고
    • SMC proteins in bacteria: Condensation motors for chromosome segregation?
    • Graumann,P.L. (2001) SMC proteins in bacteria: condensation motors for chromosome segregation? Biochimie 83, 53-59.
    • (2001) Biochimie , vol.83 , pp. 53-59
    • Graumann, P.L.1
  • 16
    • 0037124369 scopus 로고    scopus 로고
    • Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein
    • Mascarenhas,J., Soppa,J., Strunnikov,A.V. and Graumann,P.L. (2002) Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein. EMBO J., 21, 3108-3118.
    • (2002) EMBO J. , vol.21 , pp. 3108-3118
    • Mascarenhas, J.1    Soppa, J.2    Strunnikov, A.V.3    Graumann, P.L.4
  • 17
    • 0036049587 scopus 로고    scopus 로고
    • Discovery of two new families of proteins, which are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members Ypu and YpuH
    • Soppa,J., Kobayashi,K., Noirot-Gros,M.-F., Oesterhelt,D., Ehrlich,S.D., Dervyn,E., Ogasawara,N. and Moriya,S. (2002) Discovery of two new families of proteins, which are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members Ypu and YpuH. Mol. Microbiol., 45, 59-71.
    • (2002) Mol. Microbiol. , vol.45 , pp. 59-71
    • Soppa, J.1    Kobayashi, K.2    Noirot-Gros, M.-F.3    Oesterhelt, D.4    Ehrlich, S.D.5    Dervyn, E.6    Ogasawara, N.7    Moriya, S.8
  • 18
    • 0015535384 scopus 로고
    • Selective replication of bacteriophage Φ29 deoxyribonucleic acid in 6-(p-hydroxyphenylazo)-uracil-treated Bacillus subtilis
    • Schachtele,C.F., Reilly B.E., De Sain C.V., Whittington M.O. and Anderson D.L. (1973) Selective replication of bacteriophage Φ29 deoxyribonucleic acid in 6-(p-hydroxyphenylazo)-uracil-treated Bacillus subtilis. J. Virol., 11, 153-155.
    • (1973) J. Virol. , vol.11 , pp. 153-155
    • Schachtele, C.F.1    Reilly, B.E.2    De Sain, C.V.3    Whittington, M.O.4    Anderson, D.L.5
  • 20
    • 0022422712 scopus 로고
    • Overproduction of protein p6 of Bacillus subtilis phage Φ29: Role in the initiation of DNA replication
    • Pastrana,R., Lázaro,J.M., Blanco,L., García,J.A., Méndez,E. and Salas,M. (1985) Overproduction of protein p6 of Bacillus subtilis phage Φ29: role in the initiation of DNA replication. Nucleic Acids Res., 13, 3083-3100.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 3083-3100
    • Pastrana, R.1    Lázaro, J.M.2    Blanco, L.3    García, J.A.4    Mé ndez, E.5    Salas, M.6
  • 21
    • 0023056801 scopus 로고
    • Replication of phage Φ29 DNA in vitro: Role of the viral protein p6 in initiation and elongation
    • Blanco,L., Gutiérrez,J., Lázaro,J.M., Bernad,A. and Salas,M. (1986) Replication of phage Φ29 DNA in vitro: role of the viral protein p6 in initiation and elongation. Nucleic Acids Res., 14, 4923-4937.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4923-4937
    • Blanco, L.1    Gutiérrez, J.2    Lázaro, J.M.3    Bernad, A.4    Salas, M.5
  • 22
    • 0022861016 scopus 로고
    • Modulation of in vivo and in vitro transcription of bacteriophage Φ29 early genes
    • Whiteley,H.R., Ramey,W.D., Spiegelman,G.B. and Holder,R.D. (1986) Modulation of in vivo and in vitro transcription of bacteriophage Φ29 early genes. Virology, 155, 392-401.
    • (1986) Virology , vol.155 , pp. 392-401
    • Whiteley, H.R.1    Ramey, W.D.2    Spiegelman, G.B.3    Holder, R.D.4
  • 23
    • 0024579407 scopus 로고
    • In vitro transcription of bacteriophage Φ29 DNA: Inhibition of early promoters by the viral replication protein p6
    • Barthelemy,I., Mellado,R.P. and Salas,M. (1989) In vitro transcription of bacteriophage Φ29 DNA: inhibition of early promoters by the viral replication protein p6. J. Virol., 63, 460-462.
    • (1989) J. Virol. , vol.63 , pp. 460-462
    • Barthelemy, I.1    Mellado, R.P.2    Salas, M.3
  • 24
    • 0035800876 scopus 로고    scopus 로고
    • Repression of bacteriophage Φ29 early promoter C2 by viral protein p6 is due to impairment of closed complex
    • Camacho,A. and Salas,M. (2001) Repression of bacteriophage Φ29 early promoter C2 by viral protein p6 is due to impairment of closed complex. J. Biol. Chem., 276, 28927-28932.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28927-28932
    • Camacho, A.1    Salas, M.2
  • 25
    • 0039554345 scopus 로고    scopus 로고
    • Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of Φ29 early-late transcriptional switch
    • Elías-Arnanz,M. and Salas,M. (1999) Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of Φ29 early-late transcriptional switch. Genes Dev., 13, 2502-2513.
    • (1999) Genes Dev. , vol.13 , pp. 2502-2513
    • Elías-Arnanz, M.1    Salas, M.2
  • 26
    • 0025279627 scopus 로고
    • A novel nucleoprotein complex at a replication origin
    • Serrano,M., Salas,M. and Hermoso,J.M. (1990) A novel nucleoprotein complex at a replication origin. Science, 248, 1012-1016.
    • (1990) Science , vol.248 , pp. 1012-1016
    • Serrano, M.1    Salas, M.2    Hermoso, J.M.3
  • 27
    • 0027530897 scopus 로고
    • Superhelical path of the DNA in the nucleoprotein complex that activates the initiation of phage Φ29 DNA replication
    • Serrano,M., Gutiérrez,C., Salas,M. and Hermoso,J.M. (1993) Superhelical path of the DNA in the nucleoprotein complex that activates the initiation of phage Φ29 DNA replication.J. Mol. Biol., 230, 248-259.
    • (1993) J. Mol. Biol. , vol.230 , pp. 248-259
    • Serrano, M.1    Gutiérrez, C.2    Salas, M.3    Hermoso, J.M.4
  • 28
    • 2342574263 scopus 로고    scopus 로고
    • Genome wide, supercoiling-dependent, in vivo binding of a viral protein involved in DNA replication and transcriptional control
    • González-Huici,V., Salas,M. and Hermoso J.M. (2004) Genome wide, supercoiling-dependent, in vivo binding of a viral protein involved in DNA replication and transcriptional control. Nucleic Acids Res., 32, 2306-2314.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2306-2314
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3
  • 29
    • 0030612613 scopus 로고    scopus 로고
    • Phage Φ29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo
    • Abril,A.M., Salas,M., Andreu,J.M., Hermoso,J.M. and Rivas,G. (1997) Phage Φ29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo. Biochemistry, 36, 11901-11908.
    • (1997) Biochemistry , vol.36 , pp. 11901-11908
    • Abril, A.M.1    Salas, M.2    Andreu, J.M.3    Hermoso, J.M.4    Rivas, G.5
  • 30
    • 0035075425 scopus 로고    scopus 로고
    • Control of transcription by nucleoid proteins
    • McLeod,S.M. and Johnson,R.C. (2001) Control of transcription by nucleoid proteins. Curr. Opin. Microbiol., 4, 152-159.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 152-159
    • McLeod, S.M.1    Johnson, R.C.2
  • 31
    • 0037381650 scopus 로고    scopus 로고
    • Regulation of gene expression by histone-like proteins in bacteria
    • Dorman,C.J. and Deighan,P. (2003) Regulation of gene expression by histone-like proteins in bacteria. Curr. Opin. Genet. Dev., 13, 179-184.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 179-184
    • Dorman, C.J.1    Deighan, P.2
  • 33
    • 0036332716 scopus 로고    scopus 로고
    • The bacterial regulatory protein H-NS - A versatile modulator of nucleic acid structures
    • Schroder,O. and Wagner,R. (2002) The bacterial regulatory protein H-NS - a versatile modulator of nucleic acid structures. Biol. Chem., 383, 945-960.
    • (2002) Biol. Chem. , vol.383 , pp. 945-960
    • Schroder, O.1    Wagner, R.2
  • 34
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang,D.S. and Kornberg,A. (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J. Biol. Chem., 267, 23083-23086.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 35
    • 1542407109 scopus 로고    scopus 로고
    • Escherichia coli prereplication complex assembly is regulated by dynamic interplay among Fis, IHF and DnaA
    • Ryan,V.T., Grimwade,J.E., Camara,J.E., Crooke,E. and Leonard,A.C. (2004) Escherichia coli prereplication complex assembly is regulated by dynamic interplay among Fis, IHF and DnaA. Mol. Microbiol., 51, 1347-1359.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1347-1359
    • Ryan, V.T.1    Grimwade, J.E.2    Camara, J.E.3    Crooke, E.4    Leonard, A.C.5
  • 36
    • 0018824063 scopus 로고
    • Supercoils in prokaryotic DNA restrained in vivo
    • Pettijohn,D.E. and Pfenninger,O. (1980) Supercoils in prokaryotic DNA restrained in vivo. Proc. Natl Acad. Sci. USA, 77, 1331-1335.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1331-1335
    • Pettijohn, D.E.1    Pfenninger, O.2
  • 37
    • 0343240577 scopus 로고
    • Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling
    • Sinden,R.R. and Pettijohn,D.E. (1981) Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling. Proc. Natl Acad. Sci. USA, 78, 224-228.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 224-228
    • Sinden, R.R.1    Pettijohn, D.E.2
  • 38
    • 0024454856 scopus 로고
    • Signals at the bacteriophage Φ29 DNA replication origins required for protein p6 binding and activity
    • Serrano,M., Gutiérrez,J., Prieto,I., Hermoso,J.M. and Salas,M. (1989) Signals at the bacteriophage Φ29 DNA replication origins required for protein p6 binding and activity. EMBO J., 8, 1879-1885.
    • (1989) EMBO J. , vol.8 , pp. 1879-1885
    • Serrano, M.1    Gutiérrez, J.2    Prieto, I.3    Hermoso, J.M.4    Salas, M.5
  • 39
    • 0016127731 scopus 로고
    • Supressor-sensitive mutants and genetic map of Bacillus subtilis bacteriophage Φ29
    • Moreno,F., Camacho,A., Viñuela,E. and Salas,M. (1974) Supressor-sensitive mutants and genetic map of Bacillus subtilis bacteriophage Φ29. Virology, 62, 1-16.
    • (1974) Virology , vol.62 , pp. 1-16
    • Moreno, F.1    Camacho, A.2    Viñuela, E.3    Salas, M.4
  • 40
    • 0028000275 scopus 로고
    • A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage Φ29
    • Bravo,A., Hermoso,J.M. and Salas,M. (1994) A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage Φ29. Mol. Gen. Genet., 245, 529-536.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 529-536
    • Bravo, A.1    Hermoso, J.M.2    Salas, M.3
  • 41
    • 0017594209 scopus 로고
    • Assembly of Bacillus subtilis phage Φ29. 2. Mutants in the cistrons coding for the non-structural proteins
    • Jiménez,F., Camacho,A., De La Torre,J., Viñuela,E. and Salas,M. (1977) Assembly of Bacillus subtilis phage Φ29. 2. Mutants in the cistrons coding for the non-structural proteins. Eur. J. Biochem., 73, 57-72.
    • (1977) Eur. J. Biochem. , vol.73 , pp. 57-72
    • Jiménez, F.1    Camacho, A.2    De La Torre, J.3    Viñuela, E.4    Salas, M.5
  • 43
    • 0034704140 scopus 로고    scopus 로고
    • Sequence requirements for protein-primed initiation and elongation of phage Φ29 DNA replication
    • González-Huici,V., Salas,M. and Hermoso,J.M. (2000) Sequence requirements for protein-primed initiation and elongation of phage Φ29 DNA replication. J. Biol. Chem., 275, 40547-40553.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40547-40553
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3
  • 44
    • 0032489548 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial chromosome partitioning site
    • Lin,D.C.H. and Grossman,A.D. (1998) Identification and characterization of a bacterial chromosome partitioning site. Cell, 92, 675-685.
    • (1998) Cell , vol.92 , pp. 675-685
    • Lin, D.C.H.1    Grossman, A.D.2
  • 45
    • 0020695728 scopus 로고
    • Fluorescence studies of the complex formation between the gene 5 protein of bacteriophage M13 and polynucleotides
    • Alma,N.C., Harmsen,B.J., de Jong,E.A., Ven,J. and Hilbers,C.W. (1983) Fluorescence studies of the complex formation between the gene 5 protein of bacteriophage M13 and polynucleotides. J. Mol. Biol., 163, 47-62.
    • (1983) J. Mol. Biol. , vol.163 , pp. 47-62
    • Alma, N.C.1    Harmsen, B.J.2    de Jong, E.A.3    Ven, J.4    Hilbers, C.W.5
  • 46
    • 0020600546 scopus 로고
    • Thermodynamics and kinetics of co-operative protein-nucleic acid binding. I. General aspects of analysis of data
    • Schwarz,G. and Watanabe,F. (1983) Thermodynamics and kinetics of co-operative protein-nucleic acid binding. I. General aspects of analysis of data. J. Mol. Biol., 163, 467-484.
    • (1983) J. Mol. Biol. , vol.163 , pp. 467-484
    • Schwarz, G.1    Watanabe, F.2
  • 47
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee J.D. and von Hippel,P.H. (1974) Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol., 86, 469-489.
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    von Hippel, P.H.2
  • 48
    • 0028363985 scopus 로고
    • Complex formation between phage Φ29 single-stranded DNA binding protein and DNA
    • Soengas,M.S., Esteban,J.A., Salas,M. and Gutiérrez,C. (1994) Complex formation between phage Φ29 single-stranded DNA binding protein and DNA. J. Mol. Biol., 239, 213-226.
    • (1994) J. Mol. Biol. , vol.239 , pp. 213-226
    • Soengas, M.S.1    Esteban, J.A.2    Salas, M.3    Gutiérrez, C.4
  • 49
    • 0022549616 scopus 로고
    • Cooperative and noncooperative binding of protein ligands to nucleic acid lattices: Experimental approaches to the determination of thermodynamic parameters
    • Kowalczykowski,S.C., Paul,L.S., Lonberg,N., Newport,J.W., McSwiggen,J.A. and von Hippel,P.H. (1986) Cooperative and noncooperative binding of protein ligands to nucleic acid lattices: experimental approaches to the determination of thermodynamic parameters. Biochemistry, 25, 1226-1240.
    • (1986) Biochemistry , vol.25 , pp. 1226-1240
    • Kowalczykowski, S.C.1    Paul, L.S.2    Lonberg, N.3    Newport, J.W.4    McSwiggen, J.A.5    von Hippel, P.H.6
  • 50
    • 0034161329 scopus 로고    scopus 로고
    • Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation
    • Orlando,V. (2000) Mapping chromosomal proteins in vivo by formaldehyde-crosslinked-chromatin immunoprecipitation. Trends Biochem. Sci., 25, 99-104.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 99-104
    • Orlando, V.1
  • 51
    • 0023840787 scopus 로고
    • Drug-induced relaxation of supercoiled plasmid DNA in Bacillus subtilis and induction of the SOS response
    • Osburne,M.S., Zavodny,S.M. and Peterson,G.A. (1988) Drug-induced relaxation of supercoiled plasmid DNA in Bacillus subtilis and induction of the SOS response. J. Bacteriol., 170, 442-445.
    • (1988) J. Bacteriol. , vol.170 , pp. 442-445
    • Osburne, M.S.1    Zavodny, S.M.2    Peterson, G.A.3
  • 52
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosome core DNA
    • Satchwell,S.C., Drew,H.R. and Travers,A.A. (1986) Sequence periodicities in chicken nucleosome core DNA. J. Mol. Biol., 191, 659-675.
    • (1986) J. Mol. Biol. , vol.191 , pp. 659-675
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 53
    • 0024314474 scopus 로고
    • Characterization of a new prokaryotic transcriptional activator and its DNA recognition site
    • Barthelemy,I. and Salas,M. (1989) Characterization of a new prokaryotic transcriptional activator and its DNA recognition site. J. Mol. Biol., 208, 225-232.
    • (1989) J. Mol. Biol. , vol.208 , pp. 225-232
    • Barthelemy, I.1    Salas, M.2
  • 54
    • 0025323444 scopus 로고
    • Bend induced by the phage Φ29 transcriptional activator in the viral late promoter is required for activation
    • Rojo,F., Zaballos,A. and Salas,M. (1990) Bend induced by the phage Φ29 transcriptional activator in the viral late promoter is required for activation. J. Mol. Biol., 211, 713-725.
    • (1990) J. Mol. Biol. , vol.211 , pp. 713-725
    • Rojo, F.1    Zaballos, A.2    Salas, M.3
  • 57
    • 0015875908 scopus 로고
    • DNA replication in bacteriophage Φ29: The requirement of a viral-specific product for association of Φ29 DNA with the cell membrane of Bacillus amyloliquefaciens
    • Ivarie,R.D. and Pène,J.J. (1973) DNA replication in bacteriophage Φ29: the requirement of a viral-specific product for association of Φ29 DNA with the cell membrane of Bacillus amyloliquefaciens. Virology, 52, 351-362.
    • (1973) Virology , vol.52 , pp. 351-362
    • Ivarie, R.D.1    Pène, J.J.2
  • 58
    • 0031591144 scopus 로고    scopus 로고
    • Initiation of bacteriophage Φ29 DNA replication in vivo: Assembly of a membrane-associated multiprotein complex
    • Bravo,A. and Salas,M. (1997) Initiation of bacteriophage Φ29 DNA replication in vivo: Assembly of a membrane-associated multiprotein complex. J. Mol. Biol., 269, 102-112.
    • (1997) J. Mol. Biol. , vol.269 , pp. 102-112
    • Bravo, A.1    Salas, M.2
  • 59
    • 0034746227 scopus 로고    scopus 로고
    • Characterization of the bacteriophage Φ29-encoded protein p16.7: A membrane protein involved in phage DNA replication
    • Meijer,W.J.J., Serna-Rico,A. and Salas,M. (2001) Characterization of the bacteriophage Φ29-encoded protein p16.7: a membrane protein involved in phage DNA replication. Mol. Microbiol., 39, 731-746.
    • (2001) Mol. Microbiol. , vol.39 , pp. 731-746
    • Meijer, W.J.J.1    Serna-Rico, A.2    Salas, M.3
  • 60
    • 0032531536 scopus 로고    scopus 로고
    • Polymerization of bacteriophage Φ29 replication protein p1 into protofilament sheets
    • Bravo,A. and Salas,M. (1998) Polymerization of bacteriophage Φ29 replication protein p1 into protofilament sheets. EMBO J., 17, 6096-6105.
    • (1998) EMBO J. , vol.17 , pp. 6096-6105
    • Bravo, A.1    Salas, M.2
  • 61
    • 0034254279 scopus 로고    scopus 로고
    • Dynamic relocalization of phage Φ29 DNA during replication and the role of the viral protein p16.7
    • Meijer,W.J.J., Lewis,P.J., Errington,J. and Salas,M. (2000) Dynamic relocalization of phage Φ29 DNA during replication and the role of the viral protein p16.7. EMBO J., 19, 4182-4190.
    • (2000) EMBO J. , vol.19 , pp. 4182-4190
    • Meijer, W.J.J.1    Lewis, P.J.2    Errington, J.3    Salas, M.4
  • 62
    • 0034652329 scopus 로고    scopus 로고
    • Closing the ring: Links between SMC proteins and chromosome partitioning, condensation and supercoiling
    • Holmes,V.F. and Cozzarelli,N.R. (2000) Closing the ring: links between SMC proteins and chromosome partitioning, condensation and supercoiling. Proc. Natl Acad. Sci. USA, 97, 1322-1324.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1322-1324
    • Holmes, V.F.1    Cozzarelli, N.R.2
  • 63
    • 0034573198 scopus 로고    scopus 로고
    • Escherichia coli cell cycle control genes affect chromosome superhelicity
    • Weitao,T., Nordstrom,K. and Dasgupta,S. (2000) Escherichia coli cell cycle control genes affect chromosome superhelicity. EMBO Rep., 1, 494-499.
    • (2000) EMBO Rep. , vol.1 , pp. 494-499
    • Weitao, T.1    Nordstrom, K.2    Dasgupta, S.3
  • 64
    • 0032079493 scopus 로고    scopus 로고
    • Characterization of a prokaryotic SMC protein involved in chromosome partitioning
    • Britton,R.A., Lin,D.C. and Grossman,A.D. (1998) Characterization of a prokaryotic SMC protein involved in chromosome partitioning. Genes Dev., 12, 1254-1259.
    • (1998) Genes Dev. , vol.12 , pp. 1254-1259
    • Britton, R.A.1    Lin, D.C.2    Grossman, A.D.3
  • 65
    • 0033597962 scopus 로고    scopus 로고
    • 13S condensin actively reconfigures DNA by introducing global positive writhe: Implications for chromosome condensation
    • Kimura,K., Rybenkov,V.V., Crisona,N.J., Hirano,T. and Cozzarelli,N.R. (1999) 13S condensin actively reconfigures DNA by introducing global positive writhe: implications for chromosome condensation. Cell, 98, 239-248.
    • (1999) Cell , vol.98 , pp. 239-248
    • Kimura, K.1    Rybenkov, V.V.2    Crisona, N.J.3    Hirano, T.4    Cozzarelli, N.R.5
  • 66
    • 0028321033 scopus 로고
    • New concepts in protein-DNA recognition: Sequence-directed DNA bending and flexibility
    • Harrington,R.E. and Winicov,I. (1994) New concepts in protein-DNA recognition: sequence-directed DNA bending and flexibility. Prog. Nucleic Acid Res. Mol. Biol., 47, 195-270.
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.47 , pp. 195-270
    • Harrington, R.E.1    Winicov, I.2
  • 67
    • 1942501103 scopus 로고    scopus 로고
    • The push-pull mechanism of bacteriophage Φ29 DNA injection
    • González-Huici,V., Salas,M. and Hermoso J.M. (2004) The push-pull mechanism of bacteriophage Φ29 DNA injection. Mol. Microbiol., 52, 529-540.
    • (2004) Mol. Microbiol. , vol.52 , pp. 529-540
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3
  • 69
    • 0031626930 scopus 로고    scopus 로고
    • Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase
    • Rojo,F., Mencia,M., Monsalve,M. and Salas,M. (1998) Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase. Prog. Nucleic Acid Res. Mol. Biol., 60, 29-46.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.60 , pp. 29-46
    • Rojo, F.1    Mencia, M.2    Monsalve, M.3    Salas, M.4


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