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Volumn 10, Issue 9, 2010, Pages 3620-3627

One-way traffic of a viral motor channel for double-stranded DNA translocation

Author keywords

bacteriophage phi29; DNA packaging; ion channel; liposomes; membrane channel; membrane channelViral assembly; nanobiotechnology; nanomedicine; nanomotors; nanostructure; nanotechnology; rectification; Viral assembly

Indexed keywords

BACTERIOPHAGE PHI29; DNA PACKAGING; ION CHANNEL; MEMBRANE CHANNEL; NANOMEDICINES; NANOMOTORS; RECTIFICATION; VIRAL ASSEMBLY;

EID: 77956448643     PISSN: 15306984     EISSN: 15306992     Source Type: Journal    
DOI: 10.1021/nl101939e     Document Type: Article
Times cited : (84)

References (68)
  • 1
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw, W. C.; Casjens, S. R. DNA packaging by the double-stranded DNA bacteriophages Cell 1980, 21, 319-331
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 2
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29
    • Guo, P.; Peterson, C.; Anderson, D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29 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
  • 4
    • 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
  • 5
    • 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 (4) L17-L19
    • (2007) Biophys. J. , vol.93 , Issue.4
    • Sabanayagam, C.R.1    Oram, M.2    Lakowicz, J.R.3    Black, L.W.4
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 12
    • 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.; Carrascosa, J. L.; Coll, M. Detailed architecture of a DNA translocating machine: the high- resolution structure of the bacteriophage phi29 connector particle J. Mol. Biol. 2002, 315 (4) 663-676
    • (2002) J. Mol. Biol. , vol.315 , Issue.4 , pp. 663-676
    • Guasch, A.1    Pous, J.2    Ibarra, B.3    Gomis-Ruth, F.X.4    Valpuesta, J.M.5    Sousa, N.6    Carrascosa, J.L.7    Coll, M.8
  • 13
    • 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
  • 14
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage phi29 portal motor can package DNA against a large internal force
    • Smith, D. E.; Tans, S. J.; Smith, S. B.; Grimes, S.; Anderson, D. L.; Bustamante, C. The bacteriophage phi29 portal motor can package DNA against a large internal force Nature 2001, 413, 748-752
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 16
    • 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
  • 17
    • 0032565727 scopus 로고    scopus 로고
    • Bacteriophage P2 and P4 morphogenesis: Structure and function of the connector
    • Rishovd, S.; Holzenburg, A.; Johansen, B. V.; Lindqvist, B. H. Bacteriophage P2 and P4 morphogenesis: structure and function of the connector Virology 1998, 245, 11-17
    • (1998) Virology , vol.245 , pp. 11-17
    • Rishovd, S.1    Holzenburg, A.2    Johansen, B.V.3    Lindqvist, B.H.4
  • 18
    • 0034766951 scopus 로고    scopus 로고
    • The UL6 Gene Product Forms the Portal for Entry of DNA into the Herpes Simplex Virus Capsid
    • Newcomb, W. W.; Juhas, R. M.; Thomsen, D. R.; Homa, F. L.; Burch, A. D.; Weller, S. K.; Brown, J. C. The UL6 Gene Product Forms the Portal for Entry of DNA into the Herpes Simplex Virus Capsid J. Virol. 2001, 75 (22) 10923-10932
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 10923-10932
    • Newcomb, W.W.1    Juhas, R.M.2    Thomsen, D.R.3    Homa, F.L.4    Burch, A.D.5    Weller, S.K.6    Brown, J.C.7
  • 19
    • 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
  • 20
    • 0024278591 scopus 로고
    • Bacteriophage T3 connector: Three-dimensional structure and comparison with other viral head-tail connecting regions
    • Donate, L. E.; Herranz, L.; Secilla, J. P.; Carazo, J. M.; Fujisawa, H.; Carrascosa, J. L. Bacteriophage T3 connector: three-dimensional structure and comparison with other viral head-tail connecting regions J. Mol. Biol. 1988, 201, 91-100
    • (1988) J. Mol. Biol. , vol.201 , pp. 91-100
    • Donate, L.E.1    Herranz, L.2    Secilla, J.P.3    Carazo, J.M.4    Fujisawa, H.5    Carrascosa, J.L.6
  • 21
    • 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
  • 22
    • 0035718896 scopus 로고    scopus 로고
    • Molecular shuttles based on motor proteins: Active transport in synthetic environments
    • Hess, H.; Vogel, V. Molecular shuttles based on motor proteins: Active transport in synthetic environments J. Biotechnol. 2001, 82 (1) 67-85
    • (2001) J. Biotechnol. , vol.82 , Issue.1 , pp. 67-85
    • Hess, H.1    Vogel, V.2
  • 24
  • 25
    • 77956436712 scopus 로고    scopus 로고
    • Robust Properties of Membrane-Embedded Connector Channel of Bacterial Virus Phi29 DNA Packaging Motor
    • Epub ahead of print. DOI: 10.1039/C003010D
    • Jing, P.; Haque, F.; Vonderheide, A.; Montemagno, C.; Guo, P. Robust Properties of Membrane-Embedded Connector Channel of Bacterial Virus Phi29 DNA Packaging Motor. Mol. BioSyst. 2010, Epub ahead of print. DOI: 10.1039/C003010D.
    • (2010) Mol. BioSyst.
    • Jing, P.1    Haque, F.2    Vonderheide, A.3    Montemagno, C.4    Guo, P.5
  • 27
    • 67651227325 scopus 로고    scopus 로고
    • Nanobiotechnology: A fluid approach to simple circuits
    • Aguilella, V. M.; Alcaraz, A. Nanobiotechnology: A fluid approach to simple circuits Nat. Nanotechnol. 2009, 4 (7) 403-404
    • (2009) Nat. Nanotechnol. , vol.4 , Issue.7 , pp. 403-404
    • Aguilella, V.M.1    Alcaraz, A.2
  • 29
    • 63649138398 scopus 로고    scopus 로고
    • A pH-tunable nanofluidic diode with a broad range of rectifying properties
    • Ali, M.; Ramirez, P.; Mafe, S.; Neumann, R.; Ensinger, W. A pH-tunable nanofluidic diode with a broad range of rectifying properties ACS Nano 2009, 3 (3) 603-608
    • (2009) ACS Nano , vol.3 , Issue.3 , pp. 603-608
    • Ali, M.1    Ramirez, P.2    Mafe, S.3    Neumann, R.4    Ensinger, W.5
  • 30
    • 34547371450 scopus 로고    scopus 로고
    • P-n Semiconductor membrane for electrically tunable ion current rectification and filtering
    • Gracheva, M. E.; Vidal, J.; Leburton, J. P. p-n Semiconductor membrane for electrically tunable ion current rectification and filtering Nano Lett. 2007, 7 (6) 1717-1722
    • (2007) Nano Lett. , vol.7 , Issue.6 , pp. 1717-1722
    • Gracheva, M.E.1    Vidal, J.2    Leburton, J.P.3
  • 31
    • 69549137368 scopus 로고    scopus 로고
    • Nanofluidic diodes based on nanotube heterojunctions
    • Yan, R.; Liang, W.; Fan, R.; Yang, P. Nanofluidic diodes based on nanotube heterojunctions Nano Lett. 2009, 9 (11) 3820-3825
    • (2009) Nano Lett. , vol.9 , Issue.11 , pp. 3820-3825
    • Yan, R.1    Liang, W.2    Fan, R.3    Yang, P.4
  • 32
    • 34047096978 scopus 로고    scopus 로고
    • Rectification of ionic current in a nanofluidic diode
    • Karnik, R.; Duan, C.; Castelino, K.; Daiguji, H.; Majumdar, A. Rectification of ionic current in a nanofluidic diode Nano Lett. 2007, 7 (3) 547-551
    • (2007) Nano Lett. , vol.7 , Issue.3 , pp. 547-551
    • Karnik, R.1    Duan, C.2    Castelino, K.3    Daiguji, H.4    Majumdar, A.5
  • 33
    • 70350725986 scopus 로고    scopus 로고
    • Principles and applications of nanofluidic transport
    • Sparreboom, W.; van den, B. A.; Eijkel, J. C. Principles and applications of nanofluidic transport Nat. Nanotechnol. 2009, 4 (11) 713-720
    • (2009) Nat. Nanotechnol. , vol.4 , Issue.11 , pp. 713-720
    • Sparreboom, W.1    Van Den, B.A.2    Eijkel, J.C.3
  • 34
    • 76649116514 scopus 로고    scopus 로고
    • Electrostatic focusing of unlabelled DNA into nanoscale pores using a salt gradient
    • Wanunu, M.; Morrison, W.; Rabin, Y.; Grosberg, A. Y.; Meller, A. Electrostatic focusing of unlabelled DNA into nanoscale pores using a salt gradient Nat. Nanotechnol. 2010, 5, 160-165
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 160-165
    • Wanunu, M.1    Morrison, W.2    Rabin, Y.3    Grosberg, A.Y.4    Meller, A.5
  • 35
    • 0037466534 scopus 로고    scopus 로고
    • Only one pRNA hexamer but multiple copies of the DNA-packaging protein gp16 are needed for the motor to package bacterial virus phi29 genomic DNA
    • Shu, D.; Guo, P. Only one pRNA hexamer but multiple copies of the DNA-packaging protein gp16 are needed for the motor to package bacterial virus phi29 genomic DNA Virology 2003, 309 (1) 108-113
    • (2003) Virology , vol.309 , Issue.1 , pp. 108-113
    • Shu, D.1    Guo, P.2
  • 36
    • 0023660929 scopus 로고
    • Initiation events in in vitro packaging of bacteriophage φ29 DNA-gp3
    • Guo, P.; Peterson, C.; Anderson, D. Initiation events in in vitro packaging of bacteriophage φ29 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
  • 37
    • 70149115911 scopus 로고    scopus 로고
    • The Q motif of a viral packaging motor governs its force generation and communicates ATP recognition to DNA interaction
    • Tsay, J. M.; Sippy, J.; Feiss, M.; Smith, D. E. The Q motif of a viral packaging motor governs its force generation and communicates ATP recognition to DNA interaction Proc. Natl. Acad. Sci. U.S.A. 2009, 106 (34) 14355-14360
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.34 , pp. 14355-14360
    • Tsay, J.M.1    Sippy, J.2    Feiss, M.3    Smith, D.E.4
  • 38
    • 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
  • 39
    • 0019602658 scopus 로고
    • In Vitro Packaging of Bacteriophage T4 DNA
    • Black, L. W. In vitro packaging of bacteriophage T4 DNA. Virology 1981, 113, 336-344
    • (1981) Virology , vol.113 , pp. 336-344
    • Black, L.W.1
  • 40
    • 0023745657 scopus 로고
    • The source of energy for bacteriophage DNA packaging: An osmotic pump explains the data
    • Serwer, P. The source of energy for bacteriophage DNA packaging: an osmotic pump explains the data Biopolymers 1988, 27, 165-169
    • (1988) Biopolymers , vol.27 , pp. 165-169
    • Serwer, P.1
  • 41
    • 0037339538 scopus 로고    scopus 로고
    • Models of bacteriophage DNA packaging motors
    • Serwer, P. Models of bacteriophage DNA packaging motors J Struct. Biol 2003, 141 (3) 179-188
    • (2003) J Struct. Biol , vol.141 , Issue.3 , pp. 179-188
    • Serwer, P.1
  • 42
    • 0031003997 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of a Brownian motor
    • Astumian, R. D. Thermodynamics and kinetics of a Brownian motor Science 1997, 276, 917-922
    • (1997) Science , vol.276 , pp. 917-922
    • Astumian, R.D.1
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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 (5) 3864-3871
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3864-3871
    • Chen, C.1    Guo, P.2
  • 46
    • 0028960132 scopus 로고
    • Structural and functional domains of the large subunit of the bacteriophage T3 DNA packaging enzyme: Importance of the C-terminal region in prohead binding
    • Morita, M.; Tasaka, M.; Fujisawa, H. Structural and functional domains of the large subunit of the bacteriophage T3 DNA packaging enzyme: importance of the C-terminal region in prohead binding J. Mol. Biol. 1995, 245, 635-644
    • (1995) J. Mol. Biol. , vol.245 , pp. 635-644
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 47
    • 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
  • 49
    • 33845947499 scopus 로고    scopus 로고
    • Assembly of Bacteriophage Lambda Terminase into a Viral DNA Maturation and Packaging Machine
    • Maluf, N. K.; Gaussier, H.; Bogner, E.; Feiss, M.; Catalano, C. E. Assembly of Bacteriophage Lambda Terminase into a Viral DNA Maturation and Packaging Machine Biochemistry. 2006, 45, 15259-15268
    • (2006) Biochemistry. , vol.45 , pp. 15259-15268
    • Maluf, N.K.1    Gaussier, H.2    Bogner, E.3    Feiss, M.4    Catalano, C.E.5
  • 50
    • 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
  • 51
    • 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 (20) 6620-6632
    • (2008) Nucleic Acids Res. , vol.36 , Issue.20 , pp. 6620-6632
    • Xiao, F.1    Zhang, H.2    Guo, P.3
  • 52
    • 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 (4) 498-509
    • (2008) Mol. Cell , vol.31 , Issue.4 , pp. 498-509
    • Lowe, J.1    Ellonen, A.2    Allen, M.D.3    Atkinson, C.4    Sherratt, D.J.5    Grainge, I.6
  • 53
    • 33750477997 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor
    • Skordalakes, E.; Berger, J. M. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor Cell 2006, 127 (3) 553-564
    • (2006) Cell , vol.127 , Issue.3 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 54
    • 33846007717 scopus 로고    scopus 로고
    • Crystal structure of the human AAA+ protein RuvBL1
    • Matias, P. M.; Gorynia, S.; Donner, P.; Carrondo, M. A. Crystal structure of the human AAA+ protein RuvBL1 J. Biol. Chem. 2006, 281 (50) 38918-38929
    • (2006) J. Biol. Chem. , vol.281 , Issue.50 , pp. 38918-38929
    • Matias, P.M.1    Gorynia, S.2    Donner, P.3    Carrondo, M.A.4
  • 55
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • McGeoch, A. T.; Trakselis, M. A.; Laskey, R. A.; Bell, S. D. Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism Nat. Struct. Mol. Biol. 2005, 12 (9) 756-762
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.9 , pp. 756-762
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 56
    • 3042795879 scopus 로고    scopus 로고
    • Direct evidence that a conserved arginine in RuvB AAA(+) ATPase acts as an allosteric effector for the ATPase activity of the adjacent subunit in a hexamer
    • Hishida, T.; Han, Y. W.; Fujimoto, S.; Iwasaki, H.; Shinagawa, H. Direct evidence that a conserved arginine in RuvB AAA(+) ATPase acts as an allosteric effector for the ATPase activity of the adjacent subunit in a hexamer Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (26) 9573-9577
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.26 , pp. 9573-9577
    • Hishida, T.1    Han, Y.W.2    Fujimoto, S.3    Iwasaki, H.4    Shinagawa, H.5
  • 57
    • 0033570097 scopus 로고    scopus 로고
    • The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation
    • Guo, S.; Tabor, S.; Richardson, C. C. The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation J. Biol. Chem. 1999, 274 (42) 30303-30309
    • (1999) J. Biol. Chem. , vol.274 , Issue.42 , pp. 30303-30309
    • Guo, S.1    Tabor, S.2    Richardson, C.C.3
  • 58
    • 0031554722 scopus 로고    scopus 로고
    • Biochemical properties of RuvBD113N: A mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities
    • Mezard, C.; Davies, A. A.; Stasiak, A.; West, S. C. Biochemical properties of RuvBD113N: a mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities J. Mol. Biol. 1997, 271 (5) 704-717
    • (1997) J. Mol. Biol. , vol.271 , Issue.5 , pp. 704-717
    • Mezard, C.1    Davies, A.A.2    Stasiak, A.3    West, S.C.4
  • 59
    • 34248340401 scopus 로고    scopus 로고
    • Viral nanomotors for packaging of dsDNA and dsRNA
    • Guo, P. X.; 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.X.1    Lee, T.J.2
  • 61
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions
    • Tao, Y.; Olson, N. H.; Xu, W.; Anderson, D. L.; Rossmann, M. G.; Baker, T. S. Assembly of a Tailed Bacterial Virus and Its Genome Release Studied in Three Dimensions Cell 1998, 95, 431-437
    • (1998) Cell , vol.95 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 62
    • 4344657166 scopus 로고    scopus 로고
    • Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism
    • Kemp, P.; Gupta, M.; Molineux, I. J. Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism Mol. Microbiol. 2004, 53 (4) 1251-1265
    • (2004) Mol. Microbiol. , vol.53 , Issue.4 , pp. 1251-1265
    • Kemp, P.1    Gupta, M.2    Molineux, I.J.3
  • 65
    • 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 (2) 224-232
    • (2010) Virology , vol.398 , Issue.2 , pp. 224-232
    • Ray, K.1    Sabanayagam, C.R.2    Lakowicz, J.R.3    Black, L.W.4
  • 66
    • 73649146975 scopus 로고    scopus 로고
    • Single-molecule and FRET fluorescence correlation spectroscopy analyses of phage DNA packaging: Colocalization of packaged phage T4 DNA ends within the capsid
    • Ray, K.; Ma, J.; Oram, M.; Lakowicz, J. R.; Black, L. W. Single-molecule and FRET fluorescence correlation spectroscopy analyses of phage DNA packaging: colocalization of packaged phage T4 DNA ends within the capsid J. Mol. Biol. 2010, 395 (5) 1102-1113
    • (2010) J. Mol. Biol. , vol.395 , Issue.5 , pp. 1102-1113
    • Ray, K.1    Ma, J.2    Oram, M.3    Lakowicz, J.R.4    Black, L.W.5
  • 67
    • 0029039737 scopus 로고
    • Sequential interactions of structural proteins in phage phi29 procapsid assembly
    • Lee, C. S.; Guo, P. Sequential interactions of structural proteins in phage phi29 procapsid assembly J. Virol. 1995, 69, 5024-5032
    • (1995) J. Virol. , vol.69 , pp. 5024-5032
    • Lee, C.S.1    Guo, P.2
  • 68
    • 0029078936 scopus 로고
    • In vitro assembly of infectious virions of ds-DNA phage φ29 from cloned gene products and synthetic nucleic acids
    • Lee, C. S.; Guo, P. In vitro assembly of infectious virions of ds-DNA phage φ29 from cloned gene products and synthetic nucleic acids J. Virol. 1995, 69, 5018-5023
    • (1995) J. Virol. , vol.69 , pp. 5018-5023
    • Lee, C.S.1    Guo, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.