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Volumn 32, Issue 4, 2014, Pages 853-872

Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotation

Author keywords

Binary fission; Bionanomotor; Bionanotechnology; Chromosome segregation; DNA packaging; DNA repair; Holliday junction; Homologous recombination; One way traffic mechanism; Virus assembly

Indexed keywords

BACTERIOPHAGES; DNA; ROTATION;

EID: 84901951285     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2014.01.006     Document Type: Review
Times cited : (53)

References (183)
  • 2
    • 84966317575 scopus 로고
    • The anatomy of the T5 bacteriophage DNA molecule
    • Abelson J., Thomas C.A. The anatomy of the T5 bacteriophage DNA molecule. J Mol Biol 1966, 18:262-291.
    • (1966) J Mol Biol , vol.18 , pp. 262-291
    • Abelson, J.1    Thomas, C.A.2
  • 3
    • 15244343074 scopus 로고    scopus 로고
    • Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery
    • Agirrezabala X., Martin-Benito J., Valle M., Gonzalez J.M., Valencia A., Valpuesta J.M., et al. Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery. J Mol Biol 2005, 347:895-902.
    • (2005) J Mol Biol , vol.347 , pp. 895-902
    • Agirrezabala, X.1    Martin-Benito, J.2    Valle, M.3    Gonzalez, J.M.4    Valencia, A.5    Valpuesta, J.M.6
  • 4
    • 35348840808 scopus 로고    scopus 로고
    • In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using Forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy
    • Aker J., Hesselink R., Engel R., Karlova R., Borst J.W., Visser A.J.W.G., et al. In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using Forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. Plant Physiol 2007, 145:339-350.
    • (2007) Plant Physiol , vol.145 , pp. 339-350
    • Aker, J.1    Hesselink, R.2    Engel, R.3    Karlova, R.4    Borst, J.W.5    Visser, A.J.W.G.6
  • 6
    • 0037169328 scopus 로고    scopus 로고
    • FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases
    • Aussel L., Barre F.X., Aroyo M., Stasiak A., Stasiak A.Z., Sherratt D. FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell 2002, 108:195-205.
    • (2002) Cell , vol.108 , pp. 195-205
    • Aussel, L.1    Barre, F.X.2    Aroyo, M.3    Stasiak, A.4    Stasiak, A.Z.5    Sherratt, D.6
  • 7
    • 0033833423 scopus 로고    scopus 로고
    • Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage phi29
    • Badasso M.O., Leiman P.G., Tao Y., He Y., Ohlendorf D.H., Rossmann M.G., et al. Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage phi29. Acta Crystallogr D Biol Crystallogr 2000, 56(Pt 9):1187-1190.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 PART 9 , pp. 1187-1190
    • Badasso, M.O.1    Leiman, P.G.2    Tao, Y.3    He, Y.4    Ohlendorf, D.H.5    Rossmann, M.G.6
  • 8
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S., Eliason W.K., Steitz T.A. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 2007, 318:459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 9
    • 36148931768 scopus 로고    scopus 로고
    • FtsK and SpoIIIE: the tale of the conserved tails
    • Barre F.X. FtsK and SpoIIIE: the tale of the conserved tails. Mol Microbiol 2007, 66:1051-1055.
    • (2007) Mol Microbiol , vol.66 , pp. 1051-1055
    • Barre, F.X.1
  • 10
    • 0033636814 scopus 로고    scopus 로고
    • FtsK functions in the processing of a Holliday junction intermediate during bacterial chromosome segregation
    • Barre F.X., Aroyo M., Colloms S.D., Helfrich A., Cornet F., Sherratt D.J. FtsK functions in the processing of a Holliday junction intermediate during bacterial chromosome segregation. Genes Dev 2000, 14:2976-2988.
    • (2000) Genes Dev , vol.14 , pp. 2976-2988
    • Barre, F.X.1    Aroyo, M.2    Colloms, S.D.3    Helfrich, A.4    Cornet, F.5    Sherratt, D.J.6
  • 11
    • 0034602330 scopus 로고    scopus 로고
    • Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-prespore division septum
    • Bath J., Wu L.J., Errington J., Wang J.C. Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-prespore division septum. Science 2000, 290:995-997.
    • (2000) Science , vol.290 , pp. 995-997
    • Bath, J.1    Wu, L.J.2    Errington, J.3    Wang, J.C.4
  • 12
    • 33745190954 scopus 로고    scopus 로고
    • Portal fusion protein constraints on function in DNA packaging of bacteriophage T4
    • Baumann R.G., Mullaney J., Black L.W. Portal fusion protein constraints on function in DNA packaging of bacteriophage T4. Mol Microbiol 2006, 61:16-32.
    • (2006) Mol Microbiol , vol.61 , pp. 16-32
    • Baumann, R.G.1    Mullaney, J.2    Black, L.W.3
  • 13
    • 0021783271 scopus 로고
    • The DNA translocation vertex of dsDNA bacteriophages
    • Bazinet C., King J. The DNA translocation vertex of dsDNA bacteriophages. Annu Rev Microbiol 1985, 39:109-129.
    • (1985) Annu Rev Microbiol , vol.39 , pp. 109-129
    • Bazinet, C.1    King, J.2
  • 14
    • 0025078730 scopus 로고
    • The generation of concatemeric plasmid DNA in Bacillus subtilis as a consequence of bacteriophage SPP1 infection
    • Bravo A., Alonso J.C. The generation of concatemeric plasmid DNA in Bacillus subtilis as a consequence of bacteriophage SPP1 infection. Nucleic Acids Res 1990, 18:4651-4657.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4651-4657
    • Bravo, A.1    Alonso, J.C.2
  • 16
    • 33646059524 scopus 로고    scopus 로고
    • TrwB: an F(1)-ATPase-like molecular motor involved in DNA transport during bacterial conjugation
    • Cabezon E., de la C.F. TrwB: an F(1)-ATPase-like molecular motor involved in DNA transport during bacterial conjugation. Res Microbiol 2006, 157:299-305.
    • (2006) Res Microbiol , vol.157 , pp. 299-305
    • Cabezon, E.1    de la, C.F.2
  • 17
    • 73849109239 scopus 로고    scopus 로고
    • The crystal structure of bacteriophage HK97 gp6: defining a large family of head-tail connector proteins
    • Cardarelli L., Lam R., Tuite A., Baker L.A., Sadowski P.D., Radford D.R., et al. The crystal structure of bacteriophage HK97 gp6: defining a large family of head-tail connector proteins. J Mol Biol 2010, 395:754-768.
    • (2010) J Mol Biol , vol.395 , pp. 754-768
    • Cardarelli, L.1    Lam, R.2    Tuite, A.3    Baker, L.A.4    Sadowski, P.D.5    Radford, D.R.6
  • 18
    • 0020073216 scopus 로고
    • Structure of the head-tail connector of bacteriophage phi 29
    • Carrascosa J.L., Vinuela E., Garcia N., Santisteban A. Structure of the head-tail connector of bacteriophage phi 29. J Mol Biol 1982, 154:311-324.
    • (1982) J Mol Biol , vol.154 , pp. 311-324
    • Carrascosa, J.L.1    Vinuela, E.2    Garcia, N.3    Santisteban, A.4
  • 19
    • 80051707836 scopus 로고    scopus 로고
    • The DNA-packaging nanomotor of tailed bacteriophages
    • Casjens S.R. The DNA-packaging nanomotor of tailed bacteriophages. Nat Rev Microbiol 2011, 9:647-657.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 647-657
    • Casjens, S.R.1
  • 20
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar D.L.D., Klug A. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol 1962, 27:1-24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 21
    • 33748749364 scopus 로고    scopus 로고
    • Role of ATP hydrolysis in the DNA translocase activity of the bovine papillomavirus (BPV-1) E1 helicase
    • Castella S., Burgin D., Sanders C.M. Role of ATP hydrolysis in the DNA translocase activity of the bovine papillomavirus (BPV-1) E1 helicase. Nucleic Acids Res 2006, 34:3731-3741.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3731-3741
    • Castella, S.1    Burgin, D.2    Sanders, C.M.3
  • 22
    • 84877585573 scopus 로고    scopus 로고
    • SpoIIIE mechanism of directional translocation involves target search coupled to sequence-dependent motor stimulation
    • Cattoni D.I., Chara O., Godefroy C., Margeat E., Trigueros S., Milhiet P.E., et al. SpoIIIE mechanism of directional translocation involves target search coupled to sequence-dependent motor stimulation. EMBO Rep 2013, 14:473-479.
    • (2013) EMBO Rep , vol.14 , pp. 473-479
    • Cattoni, D.I.1    Chara, O.2    Godefroy, C.3    Margeat, E.4    Trigueros, S.5    Milhiet, P.E.6
  • 24
    • 54149110817 scopus 로고    scopus 로고
    • Bright-field analysis of phi29 DNA packaging motor using a magnetomechanical system
    • Chang C., Zhang H., Shu D., Guo P., Savran C. Bright-field analysis of phi29 DNA packaging motor using a magnetomechanical system. Appl Phys Lett 2008, 93:153902-153903.
    • (2008) Appl Phys Lett , vol.93 , pp. 153902-153903
    • Chang, C.1    Zhang, H.2    Shu, D.3    Guo, P.4    Savran, C.5
  • 25
    • 84899845883 scopus 로고    scopus 로고
    • Genome segregation and packaging machinery in acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus
    • [in press]
    • Chelikani V., Ranjan T., Zade A., Shukla A., Kondabagil K. Genome segregation and packaging machinery in acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus. J Virol. 2014, [in press]. 10.1128/JVI.03199-13.
    • (2014) J Virol.
    • Chelikani, V.1    Ranjan, T.2    Zade, A.3    Shukla, A.4    Kondabagil, K.5
  • 27
    • 0031060313 scopus 로고    scopus 로고
    • Magnesium-induced conformational change of packaging RNA for procapsid recognition and binding during phage phi29 DNA encapsidation
    • Chen C., Guo P. Magnesium-induced conformational change of packaging RNA for procapsid recognition and binding during phage phi29 DNA encapsidation. J Virol 1997, 71:495-500.
    • (1997) J Virol , vol.71 , pp. 495-500
    • Chen, C.1    Guo, P.2
  • 28
    • 0030896203 scopus 로고    scopus 로고
    • Sequential action of six virus-encoded DNA-packaging RNAs during phage phi29 genomic DNA translocation
    • Chen C., Guo P. Sequential action of six virus-encoded DNA-packaging RNAs during phage phi29 genomic DNA translocation. J Virol 1997, 71:3864-3871.
    • (1997) J Virol , vol.71 , pp. 3864-3871
    • Chen, C.1    Guo, P.2
  • 29
    • 0000019034 scopus 로고    scopus 로고
    • New approaches to stoichiometry determination and mechanism investigation on RNA involved in intermediate reactions
    • Chen C., Trottier M., Guo P. New approaches to stoichiometry determination and mechanism investigation on RNA involved in intermediate reactions. Nucleic Acids Symp Ser 1997, 36:190-193.
    • (1997) Nucleic Acids Symp Ser , vol.36 , pp. 190-193
    • Chen, C.1    Trottier, M.2    Guo, P.3
  • 30
    • 0036308842 scopus 로고    scopus 로고
    • The hexameric ring structure of the Escherichia coli RuvB branch migration protein
    • Chen Y.J., Yu X., Egelman E.H. The hexameric ring structure of the Escherichia coli RuvB branch migration protein. J Mol Biol 2002, 319:587-591.
    • (2002) J Mol Biol , vol.319 , pp. 587-591
    • Chen, Y.J.1    Yu, X.2    Egelman, E.H.3
  • 31
    • 84894484537 scopus 로고    scopus 로고
    • Exploiting radiation damage to map proteins in nucleoprotein complexes: The internal structure of bacteriophage T7
    • Cheng N., Wu W., Watts N.R., Steven A.C. Exploiting radiation damage to map proteins in nucleoprotein complexes: The internal structure of bacteriophage T7. J Struct Biol 2014, 185:250-256.
    • (2014) J Struct Biol , vol.185 , pp. 250-256
    • Cheng, N.1    Wu, W.2    Watts, N.R.3    Steven, A.C.4
  • 32
    • 84869987562 scopus 로고    scopus 로고
    • High degree of coordination and division of labor among subunits in a homomeric ring ATPase
    • Chistol G., Liu S., Hetherington C.L., Moffitt J.R., Grimes S., Jardine P.J., et al. High degree of coordination and division of labor among subunits in a homomeric ring ATPase. Cell 2012, 151:1017-1028.
    • (2012) Cell , vol.151 , pp. 1017-1028
    • Chistol, G.1    Liu, S.2    Hetherington, C.L.3    Moffitt, J.R.4    Grimes, S.5    Jardine, P.J.6
  • 33
    • 0036418605 scopus 로고    scopus 로고
    • Preliminary crystallographic analysis of the bacteriophage P22 portal protein
    • Cingolani G., Moore S.D., Prevelige J., Johnson J.E. Preliminary crystallographic analysis of the bacteriophage P22 portal protein. J Struct Biol 2002, 139:46-54.
    • (2002) J Struct Biol , vol.139 , pp. 46-54
    • Cingolani, G.1    Moore, S.D.2    Prevelige, J.3    Johnson, J.E.4
  • 34
    • 0242692609 scopus 로고    scopus 로고
    • The bacterial RecA protein as a motor protein
    • Cox M.M. The bacterial RecA protein as a motor protein. Annu Rev Microbiol 2003, 57:551-577.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 35
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: the fast motor that knows where it's going
    • Crozat E., Grainge I. FtsK DNA translocase: the fast motor that knows where it's going. Chembiochem 2010, 11:2232-2243.
    • (2010) Chembiochem , vol.11 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 36
    • 77951499045 scopus 로고    scopus 로고
    • Separating speed and ability to displace roadblocks during DNA translocation by FtsK
    • Crozat E., Meglio A., Allemand J.F., Chivers C.E., Howarth M., Venien-Bryan C., et al. Separating speed and ability to displace roadblocks during DNA translocation by FtsK. EMBO J 2010, 29:1423-1433.
    • (2010) EMBO J , vol.29 , pp. 1423-1433
    • Crozat, E.1    Meglio, A.2    Allemand, J.F.3    Chivers, C.E.4    Howarth, M.5    Venien-Bryan, C.6
  • 40
    • 0020475459 scopus 로고
    • Characterization of complexes between recA protein and duplex DNA by electron microscopy
    • Di C.E., Engel A., Stasiak A., Koller T. Characterization of complexes between recA protein and duplex DNA by electron microscopy. J Mol Biol 1982, 157:87-103.
    • (1982) J Mol Biol , vol.157 , pp. 87-103
    • Di, C.E.1    Engel, A.2    Stasiak, A.3    Koller, T.4
  • 41
    • 84870885884 scopus 로고    scopus 로고
    • Compression of the DNA substrate by a viral packaging motor is supported by removal of intercalating dye during translocation
    • Dixit A.B., Ray K., Black L.W. Compression of the DNA substrate by a viral packaging motor is supported by removal of intercalating dye during translocation. Proc Natl Acad Sci U S A 2012, 109:20419-20424.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 20419-20424
    • Dixit, A.B.1    Ray, K.2    Black, L.W.3
  • 42
    • 33846209611 scopus 로고    scopus 로고
    • The gpQ portal protein of bacteriophage P2 forms dodecameric connectors in crystals
    • Doan D.N., Dokland T. The gpQ portal protein of bacteriophage P2 forms dodecameric connectors in crystals. J Struct Biol 2007, 157:432-436.
    • (2007) J Struct Biol , vol.157 , pp. 432-436
    • Doan, D.N.1    Dokland, T.2
  • 43
    • 0021797403 scopus 로고
    • Structure and physical map of Rhodopseudomonas sphaeroides bacteriophage RS1 DNA
    • Donohue T.J., Chory J., Goldsand T.E., Lynn S.P., Kaplan S. Structure and physical map of Rhodopseudomonas sphaeroides bacteriophage RS1 DNA. J Virol 1985, 55:147-157.
    • (1985) J Virol , vol.55 , pp. 147-157
    • Donohue, T.J.1    Chory, J.2    Goldsand, T.E.3    Lynn, S.P.4    Kaplan, S.5
  • 44
    • 44649136828 scopus 로고    scopus 로고
    • Asymmetric EM reveals new twists in phage phi29 biology
    • Duda R.L., Conway J.F. Asymmetric EM reveals new twists in phage phi29 biology. Structure 2008, 16:831-832.
    • (2008) Structure , vol.16 , pp. 831-832
    • Duda, R.L.1    Conway, J.F.2
  • 46
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark E.J., Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 2006, 442:270-275.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 47
    • 0019378381 scopus 로고
    • DNA replication of bacteriophage T5. 3. Studies on the structure of concatemeric T5 DNA
    • Everett R.D. DNA replication of bacteriophage T5. 3. Studies on the structure of concatemeric T5 DNA. J Gen virol 1981, 52:25-38.
    • (1981) J Gen virol , vol.52 , pp. 25-38
    • Everett, R.D.1
  • 48
    • 84855423787 scopus 로고    scopus 로고
    • Role of channel lysines and "push through a one-way valve" mechanism of viral DNA packaging motor
    • Fang H., Jing P., Haque F., Guo P. Role of channel lysines and "push through a one-way valve" mechanism of viral DNA packaging motor. Biophys J 2012, 102:127-135.
    • (2012) Biophys J , vol.102 , pp. 127-135
    • Fang, H.1    Jing, P.2    Haque, F.3    Guo, P.4
  • 49
    • 84878278855 scopus 로고    scopus 로고
    • Recruitment, assembly, and molecular architecture of the SpoIIIE DNA pump revealed by superresolution microscopy
    • Fiche J.B., Cattoni D.I., Diekmann N., Langerak J.M., Clerte C., Royer C.A., et al. Recruitment, assembly, and molecular architecture of the SpoIIIE DNA pump revealed by superresolution microscopy. PLoS Biol 2013, 11:e1001557.
    • (2013) PLoS Biol , vol.11
    • Fiche, J.B.1    Cattoni, D.I.2    Diekmann, N.3    Langerak, J.M.4    Clerte, C.5    Royer, C.A.6
  • 50
    • 77953046749 scopus 로고    scopus 로고
    • Dynamic SpoIIIE assembly mediates septal membrane fission during Bacillus subtilis sporulation
    • Fleming T.C., Shin J.Y., Lee S.H., Becker E., Huang K.C., Bustamante C., et al. Dynamic SpoIIIE assembly mediates septal membrane fission during Bacillus subtilis sporulation. Genes Dev 2010, 24:1160-1172.
    • (2010) Genes Dev , vol.24 , pp. 1160-1172
    • Fleming, T.C.1    Shin, J.Y.2    Lee, S.H.3    Becker, E.4    Huang, K.C.5    Bustamante, C.6
  • 51
    • 0026323208 scopus 로고
    • Analysis of interactions among factors involved in the bacteriophage T3 DNA packaging reaction in a defined in vitro system
    • Fujisawa H., Shibata H., Kato H. Analysis of interactions among factors involved in the bacteriophage T3 DNA packaging reaction in a defined in vitro system. Virology 1991, 185:788-794.
    • (1991) Virology , vol.185 , pp. 788-794
    • Fujisawa, H.1    Shibata, H.2    Kato, H.3
  • 52
    • 84876585976 scopus 로고    scopus 로고
    • Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single- and double-stranded nucleic acids
    • Geng J., Wang S., Fang H., Guo P. Channel size conversion of Phi29 DNA-packaging nanomotor for discrimination of single- and double-stranded nucleic acids. ACS Nano 2013, 7:3315-3323.
    • (2013) ACS Nano , vol.7 , pp. 3315-3323
    • Geng, J.1    Wang, S.2    Fang, H.3    Guo, P.4
  • 53
    • 80052342523 scopus 로고    scopus 로고
    • Three reversible and controllable discrete steps of channel gating of a viral DNA packaging motor
    • Geng J., Fang H., Haque F., Zhang L., Guo P. Three reversible and controllable discrete steps of channel gating of a viral DNA packaging motor. Biomaterials 2011, 32:8234-8242.
    • (2011) Biomaterials , vol.32 , pp. 8234-8242
    • Geng, J.1    Fang, H.2    Haque, F.3    Zhang, L.4    Guo, P.5
  • 54
    • 0034923461 scopus 로고    scopus 로고
    • Structure of TrwB, a gatekeeper in bacterial conjugation
    • Gomis-Ruth F.X., Coll M. Structure of TrwB, a gatekeeper in bacterial conjugation. Int J Biochem Cell Biol 2001, 33:839-843.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 839-843
    • Gomis-Ruth, F.X.1    Coll, M.2
  • 56
    • 78650535019 scopus 로고    scopus 로고
    • Sequence-specific assembly of FtsK hexamers establishes directional translocation on DNA
    • Graham J.E., Sherratt D.J., Szczelkun M.D. Sequence-specific assembly of FtsK hexamers establishes directional translocation on DNA. Proc Natl Acad Sci U S A 2010, 107:20263-20268.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20263-20268
    • Graham, J.E.1    Sherratt, D.J.2    Szczelkun, M.D.3
  • 57
    • 52049115424 scopus 로고    scopus 로고
    • Sporulation: SpoIIIE is the key to cell differentiation
    • Grainge I. Sporulation: SpoIIIE is the key to cell differentiation. Curr Biol 2008, 18:R871-R872.
    • (2008) Curr Biol , vol.18
    • Grainge, I.1
  • 58
    • 84875389051 scopus 로고    scopus 로고
    • Simple topology: FtsK-directed recombination at the dif site
    • Grainge I. Simple topology: FtsK-directed recombination at the dif site. Biochem Soc Trans 2013, 41:595-600.
    • (2013) Biochem Soc Trans , vol.41 , pp. 595-600
    • Grainge, I.1
  • 59
    • 0031567019 scopus 로고    scopus 로고
    • The bacteriophage phi29 packaging proteins supercoil the DNA ends
    • Grimes S., Anderson D. The bacteriophage phi29 packaging proteins supercoil the DNA ends. J Mol Biol 1997, 266:901-914.
    • (1997) J Mol Biol , vol.266 , pp. 901-914
    • Grimes, S.1    Anderson, D.2
  • 60
    • 0025028872 scopus 로고
    • RNA dependence of the bateriophage phi29 DNA packaging ATPase
    • Grimes S., Anderson D. RNA dependence of the bateriophage phi29 DNA packaging ATPase. J Mol Biol 1990, 215:559-566.
    • (1990) J Mol Biol , vol.215 , pp. 559-566
    • Grimes, S.1    Anderson, D.2
  • 61
    • 79958703404 scopus 로고    scopus 로고
    • Role of phi29 connector channel loops in late-stage DNA packaging
    • Grimes S., Ma S., Gao J., Atz R., Jardine P.J. Role of phi29 connector channel loops in late-stage DNA packaging. J Mol Biol 2011, 410:50-59.
    • (2011) J Mol Biol , vol.410 , pp. 50-59
    • Grimes, S.1    Ma, S.2    Gao, J.3    Atz, R.4    Jardine, P.J.5
  • 62
    • 0036301072 scopus 로고    scopus 로고
    • Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle
    • Guasch A., Pous J., Ibarra B., Gomis-Ruth F.X., Valpuesta J.M., Sousa N., et al. Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle. J Mol Biol 2002, 315:663-676.
    • (2002) J Mol Biol , vol.315 , pp. 663-676
    • Guasch, A.1    Pous, J.2    Ibarra, B.3    Gomis-Ruth, F.X.4    Valpuesta, J.M.5    Sousa, N.6
  • 63
    • 0032516784 scopus 로고    scopus 로고
    • Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage phi29 connector particle
    • Guasch A., Pous J., Parraga A., Valpuesta J.M., Carrascosa J.L., Coll M. Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage phi29 connector particle. J Mol Biol 1998, 281:219-225.
    • (1998) J Mol Biol , vol.281 , pp. 219-225
    • Guasch, A.1    Pous, J.2    Parraga, A.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Coll, M.6
  • 64
    • 84899892055 scopus 로고    scopus 로고
    • Biophysical studies reveal new evidence for one-way revolution mechanism of biomotors (Editorial Comments: News and Notable)
    • [in press]
    • Guo P. Biophysical studies reveal new evidence for one-way revolution mechanism of biomotors (Editorial Comments: News and Notable). Biophys J 2014, [in press].
    • (2014) Biophys J
    • Guo, P.1
  • 65
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B., Onrust R., Sali A., O'Donnell M., Kuriyan J. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 1997, 91:335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 66
    • 84876817617 scopus 로고    scopus 로고
    • Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7
    • Guo F., Liu Z., Vago F., Ren Y., Wu W., Wright E.T., et al. Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7. Proc Natl Acad Sci U S A 2013, 110:6811-6816.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6811-6816
    • Guo, F.1    Liu, Z.2    Vago, F.3    Ren, Y.4    Wu, W.5    Wright, E.T.6
  • 67
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage phi29 DNA
    • Guo P., Erickson S., Anderson D. A small viral RNA is required for in vitro packaging of bacteriophage phi29 DNA. Science 1987, 236:690-694.
    • (1987) Science , vol.236 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 68
    • 0022444512 scopus 로고
    • A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage phi29
    • Guo P., Grimes S., Anderson D. A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage phi29. Proc Natl Acad Sci U S A 1986, 83:3505-3509.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3505-3509
    • Guo, P.1    Grimes, S.2    Anderson, D.3
  • 69
    • 0023660929 scopus 로고
    • Initiation events in in vitro packaging of bacteriophage phi29 DNA-gp3
    • Guo P., Peterson C., Anderson D. Initiation events in in vitro packaging of bacteriophage phi29 DNA-gp3. J Mol Biol 1987, 197:219-228.
    • (1987) J Mol Biol , vol.197 , pp. 219-228
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 70
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi29
    • Guo P., Peterson C., Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi29. J Mol Biol 1987, 197:229-236.
    • (1987) J Mol Biol , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 71
    • 84884504887 scopus 로고    scopus 로고
    • Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation
    • Guo P., Schwartz C., Haak J., Zhao Z. Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation. Virology 2013, 446:133-143.
    • (2013) Virology , vol.446 , pp. 133-143
    • Guo, P.1    Schwartz, C.2    Haak, J.3    Zhao, Z.4
  • 72
    • 0032110708 scopus 로고    scopus 로고
    • Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation
    • Guo P., Zhang C., Chen C., Trottier M., Garver K. Inter-RNA interaction of phage phi29 pRNA to form a hexameric complex for viral DNA transportation. Mol Cell 1998, 2:149-155.
    • (1998) Mol Cell , vol.2 , pp. 149-155
    • Guo, P.1    Zhang, C.2    Chen, C.3    Trottier, M.4    Garver, K.5
  • 73
    • 34248340401 scopus 로고    scopus 로고
    • Viral nanomotors for packaging of dsDNA and dsRNA
    • Guo P, Lee T.J. Viral nanomotors for packaging of dsDNA and dsRNA. Mol Microbiol 2007, 64:886-903.
    • (2007) Mol Microbiol , vol.64 , pp. 886-903
    • Guo, P.1    Lee, T.J.2
  • 74
    • 33746796409 scopus 로고    scopus 로고
    • Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex
    • Han Y.W., Tani T., Hayashi M., Hishida T., Iwasaki H., Shinagawa H., et al. Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex. Proc Natl Acad Sci U S A 2006, 103:11544-11548.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11544-11548
    • Han, Y.W.1    Tani, T.2    Hayashi, M.3    Hishida, T.4    Iwasaki, H.5    Shinagawa, H.6
  • 76
    • 0015505442 scopus 로고
    • The chromosome of bacteriophage T5. I. Analysis of the single-stranded DNA fragments by agarose gel electrophoresis
    • Hayward G.S., Smith M.G. The chromosome of bacteriophage T5. I. Analysis of the single-stranded DNA fragments by agarose gel electrophoresis. J Mol Biol 1972, 63:383-395.
    • (1972) J Mol Biol , vol.63 , pp. 383-395
    • Hayward, G.S.1    Smith, M.G.2
  • 77
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix R.W. Symmetry mismatch and DNA packaging in large bacteriophages. Proc Natl Acad Sci U S A 1978, 75:4779-4783.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 78
    • 0032563227 scopus 로고    scopus 로고
    • Bacteriophage DNA, packaging: RNA gears in a DNA transport machine (Minireview)
    • Hendrix R.W. Bacteriophage DNA, packaging: RNA gears in a DNA transport machine (Minireview). Cell 1998, 94:147-150.
    • (1998) Cell , vol.94 , pp. 147-150
    • Hendrix, R.W.1
  • 79
    • 0017698623 scopus 로고
    • DNA packaging and the pathway of bacteriophage T4 head assembly
    • Hsiao C.L., Black L.W. DNA packaging and the pathway of bacteriophage T4 head assembly. Proc Natl Acad Sci U S A 1977, 74:3652-3656.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 3652-3656
    • Hsiao, C.L.1    Black, L.W.2
  • 80
    • 84873097195 scopus 로고    scopus 로고
    • The bacteriophage T7 virion undergoes extensive structural remodeling during infection
    • Hu B., Margolin W., Molineux I.J., Liu J. The bacteriophage T7 virion undergoes extensive structural remodeling during infection. Science 2013, 339:576-579.
    • (2013) Science , vol.339 , pp. 576-579
    • Hu, B.1    Margolin, W.2    Molineux, I.J.3    Liu, J.4
  • 81
    • 33947213307 scopus 로고    scopus 로고
    • Experimental test of connector rotation during DNA packaging into bacteriophage phi29 capsids
    • Hugel T., Michaelis J., Hetherington C.L., Jardine P.J., Grimes S., Walter J.M., et al. Experimental test of connector rotation during DNA packaging into bacteriophage phi29 capsids. PloS Biol 2007, 5:558-567.
    • (2007) PloS Biol , vol.5 , pp. 558-567
    • Hugel, T.1    Michaelis, J.2    Hetherington, C.L.3    Jardine, P.J.4    Grimes, S.5    Walter, J.M.6
  • 82
    • 0029920552 scopus 로고    scopus 로고
    • Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage lambda
    • Hwang Y., Catalano C.E., Feiss M. Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage lambda. Biochemistry 1996, 35:2796-2803.
    • (1996) Biochemistry , vol.35 , pp. 2796-2803
    • Hwang, Y.1    Catalano, C.E.2    Feiss, M.3
  • 83
  • 84
    • 0035504276 scopus 로고    scopus 로고
    • Purification and functional characterization of p16, the ATPase of the bacteriophage phi29 packaging machinery
    • Ibarra B., Valpuesta J.M., Carrascosa J.L. Purification and functional characterization of p16, the ATPase of the bacteriophage phi29 packaging machinery. Nucleic Acids Res 2001, 29:4264-4273.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4264-4273
    • Ibarra, B.1    Valpuesta, J.M.2    Carrascosa, J.L.3
  • 85
    • 1942521214 scopus 로고    scopus 로고
    • The portal protein plays essential roles at different steps of the SPP1 DNA packaging process
    • Isidro A., Henriques A.O., Tavares P. The portal protein plays essential roles at different steps of the SPP1 DNA packaging process. Virology 2004, 322:253-263.
    • (2004) Virology , vol.322 , pp. 253-263
    • Isidro, A.1    Henriques, A.O.2    Tavares, P.3
  • 86
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O., Wing R.A., Eliason W.K., Wang J., Steitz T.A. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 2012, 151:267-277.
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 87
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • Iyer L.M., Makarova K.S., Koonin E.V., Aravind L. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res 2004, 32:5260-5279.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 88
    • 0018354176 scopus 로고
    • Anatomy of herpes simplex virus DNA: XII. Accumulation of head-to-tail concatemers in nuclei of infected cells and their role in the generation of the four isomeric arrangements of viral DNA
    • Jacob R.J., Morse L.S., Roizman B. Anatomy of herpes simplex virus DNA: XII. Accumulation of head-to-tail concatemers in nuclei of infected cells and their role in the generation of the four isomeric arrangements of viral DNA. J Virol 1979, 29:448-457.
    • (1979) J Virol , vol.29 , pp. 448-457
    • Jacob, R.J.1    Morse, L.S.2    Roizman, B.3
  • 89
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 2006, 439:612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 90
    • 0022927155 scopus 로고
    • Computer graphic display method for visualizing three-dimensional biological structures
    • Jimenez J., Santisteban A., Carazo J.M., Carrascosa J.L. Computer graphic display method for visualizing three-dimensional biological structures. Science 1986, 232:1113-1115.
    • (1986) Science , vol.232 , pp. 1113-1115
    • Jimenez, J.1    Santisteban, A.2    Carazo, J.M.3    Carrascosa, J.L.4
  • 91
    • 77956448643 scopus 로고    scopus 로고
    • One-way traffic of a viral motor channel for double-stranded DNA translocation
    • Jing P., Haque F., Shu D., Montemagno C., Guo P. One-way traffic of a viral motor channel for double-stranded DNA translocation. Nano Lett 2010, 10:3620-3627.
    • (2010) Nano Lett , vol.10 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Shu, D.3    Montemagno, C.4    Guo, P.5
  • 92
    • 82555176571 scopus 로고    scopus 로고
    • Players between the worlds: multifunctional DNA translocases
    • Kaimer C., Graumann P.L. Players between the worlds: multifunctional DNA translocases. Curr Opin Microbiol 2011, 14:719-725.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 719-725
    • Kaimer, C.1    Graumann, P.L.2
  • 93
    • 0033548710 scopus 로고    scopus 로고
    • DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence
    • Kaplan D.L., Steitz T.A. DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence. J Biol Chem 1999, 274:6889-6897.
    • (1999) J Biol Chem , vol.274 , pp. 6889-6897
    • Kaplan, D.L.1    Steitz, T.A.2
  • 94
    • 0035877578 scopus 로고    scopus 로고
    • A complex of the bacteriophage T7 primase-helicase and DNA polymerase directs primer utilization
    • Kato M., Frick D.N., Lee J., Tabor S., Richardson C.C., Ellenberger T. A complex of the bacteriophage T7 primase-helicase and DNA polymerase directs primer utilization. J Biol Chem 2001, 276:21809-21820.
    • (2001) J Biol Chem , vol.276 , pp. 21809-21820
    • Kato, M.1    Frick, D.N.2    Lee, J.3    Tabor, S.4    Richardson, C.C.5    Ellenberger, T.6
  • 95
    • 0017065094 scopus 로고
    • Function of gene 49 of bacteriophage T4. II. Analysis of intracellular development and the structure of very fast-sedimenting DNA
    • Kemper B., Brown D.T. Function of gene 49 of bacteriophage T4. II. Analysis of intracellular development and the structure of very fast-sedimenting DNA. J Virol 1976, 18:1000-1015.
    • (1976) J Virol , vol.18 , pp. 1000-1015
    • Kemper, B.1    Brown, D.T.2
  • 96
    • 0029156537 scopus 로고
    • Specific single-stranded breaks in mature bacteriophage T7 DNA
    • Khan S.A., Hayes S.J., Wright E.T., Watson R.H., Serwer P. Specific single-stranded breaks in mature bacteriophage T7 DNA. Virology 1995, 211:329-331.
    • (1995) Virology , vol.211 , pp. 329-331
    • Khan, S.A.1    Hayes, S.J.2    Wright, E.T.3    Watson, R.H.4    Serwer, P.5
  • 97
    • 0021632866 scopus 로고
    • Bacteriophage lambda preconnectors: purification and structure
    • Kochan J., Carrascosa J.L., Murialdo H. Bacteriophage lambda preconnectors: purification and structure. J Mol Biol 1984, 174:433-447.
    • (1984) J Mol Biol , vol.174 , pp. 433-447
    • Kochan, J.1    Carrascosa, J.L.2    Murialdo, H.3
  • 99
    • 84870589316 scopus 로고    scopus 로고
    • The dynamic pause-unpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4
    • Kottadiel V.I., Rao V.B., Chemla Y.R. The dynamic pause-unpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4. Proc Natl Acad Sci U S A 2012, 109:20000-20005.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 20000-20005
    • Kottadiel, V.I.1    Rao, V.B.2    Chemla, Y.R.3
  • 100
    • 0028308710 scopus 로고
    • Homologous pairing and DNA strand-exchange proteins
    • Kowalczykowski S.C., Eggleston A.K. Homologous pairing and DNA strand-exchange proteins. Annu Rev Biochem 1994, 63:991-1043.
    • (1994) Annu Rev Biochem , vol.63 , pp. 991-1043
    • Kowalczykowski, S.C.1    Eggleston, A.K.2
  • 101
    • 0019741697 scopus 로고
    • Defective packing of an unusual DNA in a virulent Erwinia phage, Erh 1
    • Kozloff L.M., Chapman V., DeLong S. Defective packing of an unusual DNA in a virulent Erwinia phage, Erh 1. Prog Clin Biol Res 1981, 64:253-269.
    • (1981) Prog Clin Biol Res , vol.64 , pp. 253-269
    • Kozloff, L.M.1    Chapman, V.2    DeLong, S.3
  • 102
    • 84896522348 scopus 로고    scopus 로고
    • Elastic properties and heterogeneous stiffness of the Phi29 motor connector channel
    • Kumar R., Grubmuller H. Elastic properties and heterogeneous stiffness of the Phi29 motor connector channel. Biophys J 2014, 106:1338-1348.
    • (2014) Biophys J , vol.106 , pp. 1338-1348
    • Kumar, R.1    Grubmuller, H.2
  • 103
    • 33745506037 scopus 로고    scopus 로고
    • The structure of an infectious P22 virion shows the signal for headful DNA packaging
    • Lander G.C., Tang L., Casjens S.R., Gilcrease E.B., Prevelige P., Poliakov A., et al. The structure of an infectious P22 virion shows the signal for headful DNA packaging. Science 2006, 312:1791-1795.
    • (2006) Science , vol.312 , pp. 1791-1795
    • Lander, G.C.1    Tang, L.2    Casjens, S.R.3    Gilcrease, E.B.4    Prevelige, P.5    Poliakov, A.6
  • 104
    • 34247268349 scopus 로고    scopus 로고
    • Structural framework for DNA translocation via the viral portal protein
    • Lebedev A.A., Krause M.H., Isidro A.L., Vagin A.A., Orlova E.V., Turner J., et al. Structural framework for DNA translocation via the viral portal protein. EMBO J 2007, 26:1984-1994.
    • (2007) EMBO J , vol.26 , pp. 1984-1994
    • Lebedev, A.A.1    Krause, M.H.2    Isidro, A.L.3    Vagin, A.A.4    Orlova, E.V.5    Turner, J.6
  • 105
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz J.H., McMacken R. The Escherichia coli dnaB replication protein is a DNA helicase. J Biol Chem 1986, 261:4738-4748.
    • (1986) J Biol Chem , vol.261 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 106
    • 31344436408 scopus 로고    scopus 로고
    • Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29
    • Lee T.J., Guo P. Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29. J Mol Biol 2006, 356:589-599.
    • (2006) J Mol Biol , vol.356 , pp. 589-599
    • Lee, T.J.1    Guo, P.2
  • 107
    • 70349202502 scopus 로고    scopus 로고
    • Construction of bacteriophage Phi29 DNA packaging motor and its applications in nanotechnology and therapy
    • Lee T.J., Schwartz C., Guo P. Construction of bacteriophage Phi29 DNA packaging motor and its applications in nanotechnology and therapy. Ann Biomed Eng 2009, 37:2064-2081.
    • (2009) Ann Biomed Eng , vol.37 , pp. 2064-2081
    • Lee, T.J.1    Schwartz, C.2    Guo, P.3
  • 108
    • 52049116701 scopus 로고    scopus 로고
    • Strand and nucleotide-dependent ATPase activity of gp16 of bacterial virus phi29 DNA packaging motor
    • Lee T.J., Zhang H., Liang D., Guo P. Strand and nucleotide-dependent ATPase activity of gp16 of bacterial virus phi29 DNA packaging motor. Virology 2008, 380:69-74.
    • (2008) Virology , vol.380 , pp. 69-74
    • Lee, T.J.1    Zhang, H.2    Liang, D.3    Guo, P.4
  • 110
    • 45549086385 scopus 로고    scopus 로고
    • Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain
    • Liu W., Pucci B., Rossi M., Pisani F.M., Ladenstein R. Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain. Nucleic Acids Res 2008, 36:3235-3243.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3235-3243
    • Liu, W.1    Pucci, B.2    Rossi, M.3    Pisani, F.M.4    Ladenstein, R.5
  • 111
    • 49349104892 scopus 로고    scopus 로고
    • Molecular mechanism of sequence-directed DNA loading and translocation by FtsK
    • Lowe J., Ellonen A., Allen M.D., Atkinson C., Sherratt D.J., Grainge I. Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol Cell 2008, 31:498-509.
    • (2008) Mol Cell , vol.31 , pp. 498-509
    • Lowe, J.1    Ellonen, A.2    Allen, M.D.3    Atkinson, C.4    Sherratt, D.J.5    Grainge, I.6
  • 112
    • 33745194353 scopus 로고    scopus 로고
    • Virus DNA translocation: progress towards a first ascent of mount pretty difficult
    • Maluf N.K., Feiss M. Virus DNA translocation: progress towards a first ascent of mount pretty difficult. Mol Microbiol 2006, 61:1-4.
    • (2006) Mol Microbiol , vol.61 , pp. 1-4
    • Maluf, N.K.1    Feiss, M.2
  • 113
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
    • Martin A., Baker T.A., Sauer R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 2005, 437:1115-1120.
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 114
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: structure and mechanism of hexameric FtsK
    • Massey T.H., Mercogliano C.P., Yates J., Sherratt D.J., Lowe J. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol Cell 2006, 23:457-469.
    • (2006) Mol Cell , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Lowe, J.5
  • 115
    • 77952897504 scopus 로고    scopus 로고
    • The conjugative DNA translocase TrwB is a structure-specific DNA-binding protein
    • Matilla I., Alfonso C., Rivas G., Bolt E.L., de la C.F., Cabezon E. The conjugative DNA translocase TrwB is a structure-specific DNA-binding protein. J Biol Chem 2010, 285:17537-17544.
    • (2010) J Biol Chem , vol.285 , pp. 17537-17544
    • Matilla, I.1    Alfonso, C.2    Rivas, G.3    Bolt, E.L.4    de la, C.F.5    Cabezon, E.6
  • 116
    • 63849109732 scopus 로고    scopus 로고
    • Mechanism of replication machinery assembly as revealed by the DNA ligase-PCNA-DNA complex architecture
    • Mayanagi K., Kiyonari S., Saito M., Shirai T., Ishino Y., Morikawa K. Mechanism of replication machinery assembly as revealed by the DNA ligase-PCNA-DNA complex architecture. Proc Natl Acad Sci U S A 2009, 106:4647-4652.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4647-4652
    • Mayanagi, K.1    Kiyonari, S.2    Saito, M.3    Shirai, T.4    Ishino, Y.5    Morikawa, K.6
  • 118
    • 0022429092 scopus 로고
    • Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors
    • Menetski J.P., Kowalczykowski S.C. Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors. J Mol Biol 1985, 181:281-295.
    • (1985) J Mol Biol , vol.181 , pp. 281-295
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 120
    • 85027930977 scopus 로고    scopus 로고
    • Popping the cork: mechanisms of phage genome ejection
    • Molineux I.J., Panja D. Popping the cork: mechanisms of phage genome ejection. Nat Rev Microbiol 2013, 11:194-204.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 194-204
    • Molineux, I.J.1    Panja, D.2
  • 121
    • 38449092849 scopus 로고    scopus 로고
    • Grouping of ferritin and gold nanoparticles conjugated to pRNA of the phage phi29 DNA-packaging motor
    • Moll D., Guo P. Grouping of ferritin and gold nanoparticles conjugated to pRNA of the phage phi29 DNA-packaging motor. J Nanosci Nanotechnol 2007, 7:3257-3267.
    • (2007) J Nanosci Nanotechnol , vol.7 , pp. 3257-3267
    • Moll, D.1    Guo, P.2
  • 122
    • 22044451059 scopus 로고    scopus 로고
    • Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29
    • Moll W.-D., Guo P. Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29. J Mol Biol 2005, 351:100-107.
    • (2005) J Mol Biol , vol.351 , pp. 100-107
    • Moll, W.-D.1    Guo, P.2
  • 123
    • 4344610198 scopus 로고    scopus 로고
    • DNA binding properties of protein TrwA, a possible structural variant of the Arc repressor superfamily
    • Moncalian G., de la C.F. DNA binding properties of protein TrwA, a possible structural variant of the Arc repressor superfamily. Biochim Biophys Acta 2004, 1701:15-23.
    • (2004) Biochim Biophys Acta , vol.1701 , pp. 15-23
    • Moncalian, G.1    de la, C.F.2
  • 124
  • 125
    • 0035783057 scopus 로고    scopus 로고
    • Cryoelectron-microscopy image reconstruction of symmetry mismatches in bacteriophage phi29
    • Morais M.C., Tao Y., Olsen N.H., Grimes S., Jardine P.J., Anderson D., et al. Cryoelectron-microscopy image reconstruction of symmetry mismatches in bacteriophage phi29. J Struct Biol 2001, 135:38-46.
    • (2001) J Struct Biol , vol.135 , pp. 38-46
    • Morais, M.C.1    Tao, Y.2    Olsen, N.H.3    Grimes, S.4    Jardine, P.J.5    Anderson, D.6
  • 126
    • 0027299633 scopus 로고
    • DNA packaging ATPase of bacteriophage T3
    • Morita M., Tasaka M., Fujisawa H. DNA packaging ATPase of bacteriophage T3. Virology 1993, 193:748-752.
    • (1993) Virology , vol.193 , pp. 748-752
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 128
    • 0035936698 scopus 로고    scopus 로고
    • Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010
    • Niedenzu T., Röleke D., Bains G., Scherzinger E., Saenger W. Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010. J Mol Biol 2001, 306:479-487.
    • (2001) J Mol Biol , vol.306 , pp. 479-487
    • Niedenzu, T.1    Röleke, D.2    Bains, G.3    Scherzinger, E.4    Saenger, W.5
  • 130
    • 46649088725 scopus 로고    scopus 로고
    • Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure
    • Oram M., Sabanayagam C., Black L.W. Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure. J Mol Biol 2008, 381:61-72.
    • (2008) J Mol Biol , vol.381 , pp. 61-72
    • Oram, M.1    Sabanayagam, C.2    Black, L.W.3
  • 131
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy
    • Orlova E.V., Gowen B., Droge A., Stiege A., Weise F., Lurz R., et al. Structure of a viral DNA gatekeeper at 10 A resolution by cryo-electron microscopy. EMBO J 2003, 22:1255-1262.
    • (2003) EMBO J , vol.22 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Droge, A.3    Stiege, A.4    Weise, F.5    Lurz, R.6
  • 132
    • 33645986125 scopus 로고    scopus 로고
    • Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively bind and bend viral DNA: implications for the assembly of a genome-packaging motor
    • Ortega M.E., Catalano C.E. Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively bind and bend viral DNA: implications for the assembly of a genome-packaging motor. Biochemistry 2006, 45:5180-5189.
    • (2006) Biochemistry , vol.45 , pp. 5180-5189
    • Ortega, M.E.1    Catalano, C.E.2
  • 133
    • 79551502787 scopus 로고    scopus 로고
    • Dynamics of bacteriophage genome ejection in vitro and in vivo
    • Panja D., Molineux I.J. Dynamics of bacteriophage genome ejection in vitro and in vivo. Phys Biol 2010, 7:045006.
    • (2010) Phys Biol , vol.7 , pp. 045006
    • Panja, D.1    Molineux, I.J.2
  • 134
    • 0023856652 scopus 로고
    • Effects of DNA heterologies on bacteriophage lambda packaging
    • Pearson R.K., Fox M.S. Effects of DNA heterologies on bacteriophage lambda packaging. Genetics 1988, 118:5-12.
    • (1988) Genetics , vol.118 , pp. 5-12
    • Pearson, R.K.1    Fox, M.S.2
  • 136
    • 47749092360 scopus 로고    scopus 로고
    • Packaging double-helical DNA into viral capsids: structures, forces, and energetics
    • Petrov A.S., Harvey S.C. Packaging double-helical DNA into viral capsids: structures, forces, and energetics. Biophys J 2008, 95:497-502.
    • (2008) Biophys J , vol.95 , pp. 497-502
    • Petrov, A.S.1    Harvey, S.C.2
  • 137
    • 79952437811 scopus 로고    scopus 로고
    • Role of DNA-DNA interactions on the structure and thermodynamics of bacteriophages Lambda and P4
    • Petrov A.S., Harvey S.C. Role of DNA-DNA interactions on the structure and thermodynamics of bacteriophages Lambda and P4. J Struct Biol 2011, 174:137-146.
    • (2011) J Struct Biol , vol.174 , pp. 137-146
    • Petrov, A.S.1    Harvey, S.C.2
  • 138
    • 0029806695 scopus 로고    scopus 로고
    • Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction
    • Rafferty J.B., Sedelnikova S.E., Hargreaves D., Artymiuk P.J., Baker P.J., Sharples G.J., et al. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science 1996, 274:415-421.
    • (1996) Science , vol.274 , pp. 415-421
    • Rafferty, J.B.1    Sedelnikova, S.E.2    Hargreaves, D.3    Artymiuk, P.J.4    Baker, P.J.5    Sharples, G.J.6
  • 139
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao V.B., Feiss M. The bacteriophage DNA packaging motor. Annu Rev Genet 2008, 42:647-681.
    • (2008) Annu Rev Genet , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 140
    • 75849131151 scopus 로고    scopus 로고
    • DNA crunching by a viral packaging motor: compression of a procapsid-portal stalled Y-DNA substrate
    • Ray K., Sabanayagam C.R., Lakowicz J.R., Black L.W. DNA crunching by a viral packaging motor: compression of a procapsid-portal stalled Y-DNA substrate. Virology 2010, 398:224-232.
    • (2010) Virology , vol.398 , pp. 224-232
    • Ray, K.1    Sabanayagam, C.R.2    Lakowicz, J.R.3    Black, L.W.4
  • 141
    • 0022443399 scopus 로고
    • Presence of random single-strand gaps in mycobacteriophage I3 DNA
    • Reddy A.B., Gopinathan K.P. Presence of random single-strand gaps in mycobacteriophage I3 DNA. Gene 1986, 44:227-234.
    • (1986) Gene , vol.44 , pp. 227-234
    • Reddy, A.B.1    Gopinathan, K.P.2
  • 142
    • 34548216327 scopus 로고    scopus 로고
    • Viral DNA packaging studied by fluorescence correlation spectroscopy
    • Sabanayagam C.R., Oram M., Lakowicz J.R., Black L.W. Viral DNA packaging studied by fluorescence correlation spectroscopy. Biophys J 2007, 93:L17-L19.
    • (2007) Biophys J , vol.93
    • Sabanayagam, C.R.1    Oram, M.2    Lakowicz, J.R.3    Black, L.W.4
  • 143
    • 84879785627 scopus 로고    scopus 로고
    • The ATPase of the phi29 DNA-packaging motor is a member of the hexameric AAA+ superfamily
    • Schwartz C., De Donatis G.M., Fang H., Guo P. The ATPase of the phi29 DNA-packaging motor is a member of the hexameric AAA+ superfamily. Virology 2013, 443:20-27.
    • (2013) Virology , vol.443 , pp. 20-27
    • Schwartz, C.1    De Donatis, G.M.2    Fang, H.3    Guo, P.4
  • 144
    • 84879787373 scopus 로고    scopus 로고
    • Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling
    • Schwartz C., De Donatis G.M., Zhang H., Fang H., Guo P. Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling. Virology 2013, 443:28-39.
    • (2013) Virology , vol.443 , pp. 28-39
    • Schwartz, C.1    De Donatis, G.M.2    Zhang, H.3    Fang, H.4    Guo, P.5
  • 145
    • 84859298657 scopus 로고    scopus 로고
    • Sequential action of ATPase, ATP, ADP, Pi and dsDNA in procapsid-free system to enlighten mechanism in viral dsDNA packaging
    • Schwartz C., Fang H., Huang L., Guo P. Sequential action of ATPase, ATP, ADP, Pi and dsDNA in procapsid-free system to enlighten mechanism in viral dsDNA packaging. Nucleic Acids Res 2012, 40:2577-2586.
    • (2012) Nucleic Acids Res , vol.40 , pp. 2577-2586
    • Schwartz, C.1    Fang, H.2    Huang, L.3    Guo, P.4
  • 146
    • 0037339538 scopus 로고    scopus 로고
    • Models of bacteriophage DNA packaging motors
    • Serwer P. Models of bacteriophage DNA packaging motors. J Struct Biol 2003, 141:179-188.
    • (2003) J Struct Biol , vol.141 , pp. 179-188
    • Serwer, P.1
  • 147
    • 79952154608 scopus 로고    scopus 로고
    • A hypothesis for bacteriophage DNA packaging motors
    • Serwer P. A hypothesis for bacteriophage DNA packaging motors. Viruses 2010, 2:1821-1843.
    • (2010) Viruses , vol.2 , pp. 1821-1843
    • Serwer, P.1
  • 148
    • 0037016404 scopus 로고    scopus 로고
    • Role of cell-specific SpoIIIE assembly in polarity of DNA transfer
    • Sharp M.D., Pogliano K. Role of cell-specific SpoIIIE assembly in polarity of DNA transfer. Science 2002, 295:137-139.
    • (2002) Science , vol.295 , pp. 137-139
    • Sharp, M.D.1    Pogliano, K.2
  • 149
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single molecule dual-view system
    • Shu D., Zhang H., Jin J., Guo P. Counting of six pRNAs of phi29 DNA-packaging motor with customized single molecule dual-view system. EMBO J 2007, 26:527-537.
    • (2007) EMBO J , vol.26 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 150
    • 84883203978 scopus 로고    scopus 로고
    • Fabrication of pRNA nanoparticles to deliver therapeutic RNAs and bioactive compounds into tumor cells
    • Shu Y., Shu D., Haque F., Guo P. Fabrication of pRNA nanoparticles to deliver therapeutic RNAs and bioactive compounds into tumor cells. Nat Protoc 2013, 8:1635-1659.
    • (2013) Nat Protoc , vol.8 , pp. 1635-1659
    • Shu, Y.1    Shu, D.2    Haque, F.3    Guo, P.4
  • 151
    • 84878025754 scopus 로고    scopus 로고
    • Fabrication of 14 different RNA nanoparticles for specific tumor targeting without accumulation in normal organs
    • Shu Y., Haque F., Shu D., Li W., Zhu Z., Kotb M., et al. Fabrication of 14 different RNA nanoparticles for specific tumor targeting without accumulation in normal organs. RNA 2013, 19:766-777.
    • (2013) RNA , vol.19 , pp. 766-777
    • Shu, Y.1    Haque, F.2    Shu, D.3    Li, W.4    Zhu, Z.5    Kotb, M.6
  • 154
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 2000, 101:589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 156
    • 39449115385 scopus 로고    scopus 로고
    • AAA+ proteins: diversity in function, similarity in structure
    • Snider J., Houry W.A. AAA+ proteins: diversity in function, similarity in structure. Biochem Soc Trans 2008, 36:72-77.
    • (2008) Biochem Soc Trans , vol.36 , pp. 72-77
    • Snider, J.1    Houry, W.A.2
  • 157
    • 65149084160 scopus 로고    scopus 로고
    • The AAA+ superfamily of functionally diverse proteins
    • Snider J., Thibault G., Houry W.A. The AAA+ superfamily of functionally diverse proteins. Genome Biol 2008, 9:216.
    • (2008) Genome Biol , vol.9 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 158
    • 0023830654 scopus 로고
    • Concatemerization and packaging of bacteriophage T7 DNA in vitro: determination of the concatemers' length and appearance kinetics by use of rotating gell electrophoresis
    • Son M., Hayes S.J., Serwer P. Concatemerization and packaging of bacteriophage T7 DNA in vitro: determination of the concatemers' length and appearance kinetics by use of rotating gell electrophoresis. Virology 1988, 162:38-46.
    • (1988) Virology , vol.162 , pp. 38-46
    • Son, M.1    Hayes, S.J.2    Serwer, P.3
  • 159
    • 57649228017 scopus 로고    scopus 로고
    • The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces
    • Sun S., Kondabagil K., Draper B., Alam T.I., Bowman V.D., Zhang Z., et al. The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces. Cell 2008, 135:1251-1262.
    • (2008) Cell , vol.135 , pp. 1251-1262
    • Sun, S.1    Kondabagil, K.2    Draper, B.3    Alam, T.I.4    Bowman, V.D.5    Zhang, Z.6
  • 161
    • 33947281384 scopus 로고    scopus 로고
    • The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids
    • Sun S.Y., Kondabagil K., Gentz P.M., Rossmann M.G., Rao V.B. The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol Cell 2007, 25:943-949.
    • (2007) Mol Cell , vol.25 , pp. 943-949
    • Sun, S.Y.1    Kondabagil, K.2    Gentz, P.M.3    Rossmann, M.G.4    Rao, V.B.5
  • 163
    • 34548489399 scopus 로고    scopus 로고
    • The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: implications for a common assembly mechanism of DNA translocating motors
    • Tato I., Matilla I., Arechaga I., Zunzunegui S., de la C.F., Cabezon E. The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: implications for a common assembly mechanism of DNA translocating motors. J Biol Chem 2007, 282:25569-25576.
    • (2007) J Biol Chem , vol.282 , pp. 25569-25576
    • Tato, I.1    Matilla, I.2    Arechaga, I.3    Zunzunegui, S.4    de la, C.F.5    Cabezon, E.6
  • 164
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase
    • Tato I., Zunzunegui S., de la C.F., Cabezon E. TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase. Proc Natl Acad Sci U S A 2005, 102:8156-8161.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    de la, C.F.3    Cabezon, E.4
  • 165
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: the structural basis for translocation polarity in hexameric helicases
    • Thomsen N.D., Berger J.M. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 2009, 139:523-534.
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 166
    • 0031060162 scopus 로고    scopus 로고
    • Approaches to determine stoichiometry of viral assembly components
    • Trottier M., Guo P. Approaches to determine stoichiometry of viral assembly components. J Virol 1997, 71:487-494.
    • (1997) J Virol , vol.71 , pp. 487-494
    • Trottier, M.1    Guo, P.2
  • 167
    • 0028000731 scopus 로고
    • Structure of viral connectors and their function in bacteriophage assembly and DNA packaging
    • Valpuesta J.M., Carrascosa J. Structure of viral connectors and their function in bacteriophage assembly and DNA packaging. Q Rev Biophys 1994, 27:107-155.
    • (1994) Q Rev Biophys , vol.27 , pp. 107-155
    • Valpuesta, J.M.1    Carrascosa, J.2
  • 168
    • 0026532074 scopus 로고
    • Three-dimensional structure of T3 connector purified from overexpressing bacteria
    • Valpuesta J.M., Fujisawa H., Marco S., Carazo J.M., Carrascosa J. Three-dimensional structure of T3 connector purified from overexpressing bacteria. J Mol Biol 1992, 224:103-112.
    • (1992) J Mol Biol , vol.224 , pp. 103-112
    • Valpuesta, J.M.1    Fujisawa, H.2    Marco, S.3    Carazo, J.M.4    Carrascosa, J.5
  • 169
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang F., Mei Z., Qi Y., Yan C., Hu Q., Wang J., et al. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 2011, 471:331-335.
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3    Yan, C.4    Hu, Q.5    Wang, J.6
  • 170
    • 0023664536 scopus 로고
    • Processing of concatemers of bacteriophage T7 DNA in vitro
    • White J.H., Richardson C.C. Processing of concatemers of bacteriophage T7 DNA in vitro. J Biol Chem 1987, 262:8854-8860.
    • (1987) J Biol Chem , vol.262 , pp. 8854-8860
    • White, J.H.1    Richardson, C.C.2
  • 171
    • 1642265785 scopus 로고    scopus 로고
    • EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA(+) hexamer
    • Willows R.D., Hansson A., Birch D., Al-Karadaghi S., Hansson M. EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA(+) hexamer. J Struct Biol 2004, 146:227-233.
    • (2004) J Struct Biol , vol.146 , pp. 227-233
    • Willows, R.D.1    Hansson, A.2    Birch, D.3    Al-Karadaghi, S.4    Hansson, M.5
  • 172
    • 56649091437 scopus 로고    scopus 로고
    • Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging
    • Xiao F., Zhang H., Guo P. Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging. Nucleic Acids Res 2008, 36:6620-6632.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6620-6632
    • Xiao, F.1    Zhang, H.2    Guo, P.3
  • 173
    • 4444308700 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in a compressed helical filament
    • Xing X., Bell C.E. Crystal structures of Escherichia coli RecA in a compressed helical filament. J Mol Biol 2004, 342:1471-1485.
    • (2004) J Mol Biol , vol.342 , pp. 1471-1485
    • Xing, X.1    Bell, C.E.2
  • 174
    • 11144255128 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP
    • Xing X., Bell C.E. Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP. Biochemistry 2004, 43:16142-16152.
    • (2004) Biochemistry , vol.43 , pp. 16142-16152
    • Xing, X.1    Bell, C.E.2
  • 176
    • 0031786575 scopus 로고    scopus 로고
    • Role of the C terminus of FtsK in Escherichia coli chromosome segregation
    • Yu X.C., Weihe E.K., Margolin W. Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J Bacteriol 1998, 180:6424-6428.
    • (1998) J Bacteriol , vol.180 , pp. 6424-6428
    • Yu, X.C.1    Weihe, E.K.2    Margolin, W.3
  • 177
    • 0019720768 scopus 로고
    • DNA ligase is required for encapsidation of bacteriophage T4 DNA
    • Zachary A., Black L.W. DNA ligase is required for encapsidation of bacteriophage T4 DNA. J Mol Biol 1981, 149:641-658.
    • (1981) J Mol Biol , vol.149 , pp. 641-658
    • Zachary, A.1    Black, L.W.2
  • 178
    • 0022502180 scopus 로고
    • Topoisomerase II and other DNA-delay and DNA-arrest mutations impair bacteriophage T4 DNA packaging in vivo and in vitro
    • Zachary A., Black L.W. Topoisomerase II and other DNA-delay and DNA-arrest mutations impair bacteriophage T4 DNA packaging in vivo and in vitro. J Virol 1986, 60:97-104.
    • (1986) J Virol , vol.60 , pp. 97-104
    • Zachary, A.1    Black, L.W.2
  • 180
    • 84862878463 scopus 로고    scopus 로고
    • "Push through one-way valve" mechanism of viral DNA packaging
    • Zhang H., Schwartz C., De Donatis G.M., Guo P. "Push through one-way valve" mechanism of viral DNA packaging. Adv Virus Res 2012, 83:415-465.
    • (2012) Adv Virus Res , vol.83 , pp. 415-465
    • Zhang, H.1    Schwartz, C.2    De Donatis, G.M.3    Guo, P.4
  • 181
    • 84883203974 scopus 로고    scopus 로고
    • Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA
    • Zhang H., Endrizzi J.A., Shu Y., Haque F., Sauter C., Shlyakhtenko L.S., et al. Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA. RNA 2013, 19:1226-1237.
    • (2013) RNA , vol.19 , pp. 1226-1237
    • Zhang, H.1    Endrizzi, J.A.2    Shu, Y.3    Haque, F.4    Sauter, C.5    Shlyakhtenko, L.S.6
  • 182
    • 0034737313 scopus 로고    scopus 로고
    • Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy
    • Zhang Z., Greene B., Thuman-Commike P.A., Jakana J., Prevelige P.E., King J., et al. Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy. J Mol Biol 2000, 297:615-626.
    • (2000) J Mol Biol , vol.297 , pp. 615-626
    • Zhang, Z.1    Greene, B.2    Thuman-Commike, P.A.3    Jakana, J.4    Prevelige, P.E.5    King, J.6
  • 183
    • 84878292282 scopus 로고    scopus 로고
    • Mechanism of one-way traffic of hexameric Phi29 DNA packaging motor with four electropositive relaying layers facilitating anti-parallel revolution
    • Zhao Z., Khisamutdinov E., Schwartz C., Guo P. Mechanism of one-way traffic of hexameric Phi29 DNA packaging motor with four electropositive relaying layers facilitating anti-parallel revolution. ACS Nano 2013, 7:4082-4092.
    • (2013) ACS Nano , vol.7 , pp. 4082-4092
    • Zhao, Z.1    Khisamutdinov, E.2    Schwartz, C.3    Guo, P.4


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