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Volumn 309, Issue 1, 2003, Pages 108-113

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

Author keywords

ATPase; DNA packaging; DNA packaging intermediates; Nanomotor; Proccessivity; RNA structure; Viral assembly; Viral assembly intermediates

Indexed keywords

ADENOSINE TRIPHOSPHATE; GENOMIC DNA; GLYCOPROTEIN GP 16; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS RNA;

EID: 0037466534     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0042-6822(03)00011-4     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 0017737569 scopus 로고
    • Early events in the in vitro packaging of bacteriophage lambda DNA
    • Becker A., Marko M., Gold M. Early events in the in vitro packaging of bacteriophage lambda DNA. Virology. 78:1977;291-305.
    • (1977) Virology , vol.78 , pp. 291-305
    • Becker, A.1    Marko, M.2    Gold, M.3
  • 2
    • 0027260609 scopus 로고
    • Packaging capacity and stability of human adenovirus type 5 vectors
    • Bett A., Prevec L., Graham F. Packaging capacity and stability of human adenovirus type 5 vectors. J. Virol. 67:1993;5911-5921.
    • (1993) J. Virol. , vol.67 , pp. 5911-5921
    • Bett, A.1    Prevec, L.2    Graham, F.3
  • 3
    • 0024452966 scopus 로고
    • DNA packaging in dsDNA bacteriophages
    • Black L.W. DNA packaging in dsDNA bacteriophages. Ann. Rev. Microbiol. 43:1989;267-292.
    • (1989) Ann. Rev. Microbiol. , vol.43 , pp. 267-292
    • Black, L.W.1
  • 4
    • 0031800615 scopus 로고    scopus 로고
    • DNA package mutant: Repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles
    • Cassetti M.C., Merchlinsky M., Wolffe E.J., Weiserg A.S., Moss B. DNA package mutant repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles . J. Virol. 72:(7):1998;5769-5780.
    • (1998) J. Virol. , vol.72 , Issue.7 , pp. 5769-5780
    • Cassetti, M.C.1    Merchlinsky, M.2    Wolffe, E.J.3    Weiserg, A.S.4    Moss, B.5
  • 5
    • 0029129145 scopus 로고
    • Virus DNA packaging: The strategy used by phage λ
    • Catalano C.E., Cue D., Feiss M. Virus DNA packaging the strategy used by phage λ Mol. Microbiol. 16:1995;1075-1086.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 6
    • 0032519891 scopus 로고    scopus 로고
    • Evolution of Streptococcus thermophilus bacteriophage genomes by modular exchanges followed by point mutations and small deletions and insertions
    • Desiere F., Lucchini S., Brussow H. Evolution of Streptococcus thermophilus bacteriophage genomes by modular exchanges followed by point mutations and small deletions and insertions. Virology. 241:1998;345-356.
    • (1998) Virology , vol.241 , pp. 345-356
    • Desiere, F.1    Lucchini, S.2    Brussow, H.3
  • 7
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn J.J., Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166:1983;477-535.
    • (1983) J. Mol. Biol. , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 8
    • 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. 21:1980;319-331.
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 9
    • 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. 315:2002;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    Carrascosa, J.L.7    Coll, M.8
  • 10
    • 34248333990 scopus 로고
    • Introduction: Principles, perspectives, and potential applications in viral assembly
    • Guo P. Introduction principles, perspectives, and potential applications in viral assembly . Sem. Virol. (Ed. Intro.). 5:(1):1994;1-3.
    • (1994) Sem. Virol. (Ed. Intro.) , vol.5 , Issue.1 , pp. 1-3
    • Guo, P.1
  • 11
    • 0036043690 scopus 로고    scopus 로고
    • Structure and function of phi29 hexameric RNA that drive viral DNA packaging motor: Review
    • Guo P. Structure and function of phi29 hexameric RNA that drive viral DNA packaging motor review . Prog. Nucl Acid Res Mol. Biol. 72:2002;415-472.
    • (2002) Prog. Nucl Acid Res Mol. Biol. , vol.72 , pp. 415-472
    • Guo, P.1
  • 12
    • 0022444512 scopus 로고
    • A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage φ29
    • Guo P., Grimes S., Anderson D. A defined system for in vitro packaging of DNA-gp3 of the Bacillus subtilis bacteriophage φ29. Proc. Natl. Acad. Sci. USA. 83:1986;3505-3509.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3505-3509
    • Guo, P.1    Grimes, S.2    Anderson, D.3
  • 13
    • 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. 197:1987;229-236.
    • (1987) J. Mol. Biol. , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 14
    • 0025925179 scopus 로고
    • SRNA of bacteriophage φ29 of B.subtilis mediates DNA packaging of φ29 proheads assembled in E. coli
    • Guo P., Rajogopal B., Anderson D., Erickson S., Lee C.-S. sRNA of bacteriophage φ29 of B.subtilis mediates DNA packaging of φ29 proheads assembled in E. coli. Virology. 185:1991;395-400.
    • (1991) Virology , vol.185 , pp. 395-400
    • Guo, P.1    Rajogopal, B.2    Anderson, D.3    Erickson, S.4    Lee, C.-S.5
  • 15
    • 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. 2:1998;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
  • 16
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney D.D. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature. 377:1995;448-450.
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 17
    • 0035804245 scopus 로고    scopus 로고
    • Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase
    • Harada Y., Ohara O., Takatsuki A., Itoh H., Shimamoto N., Kinosita K. Jr. Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase. Nature. 409:2001;113-115.
    • (2001) Nature , vol.409 , pp. 113-115
    • Harada, Y.1    Ohara, O.2    Takatsuki, A.3    Itoh, H.4    Shimamoto, N.5    Kinosita K., Jr.6
  • 18
    • 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. 94:1998;147-150.
    • (1998) Cell , vol.94 , pp. 147-150
    • Hendrix, R.W.1
  • 19
    • 0037036444 scopus 로고    scopus 로고
    • Computer modeling of three-dimensional structure of DNA-packaging RNA(pRNA) monomer, dimer, and hexamer of Phi29 DNA packaging motor
    • Hoeprich S., Guo P. Computer modeling of three-dimensional structure of DNA-packaging RNA(pRNA) monomer, dimer, and hexamer of Phi29 DNA packaging motor. J Biol. Chem. 277:(23):2002;20794-20803.
    • (2002) J Biol. Chem. , vol.277 , Issue.23 , pp. 20794-20803
    • Hoeprich, S.1    Guo, P.2
  • 20
    • 0035504276 scopus 로고    scopus 로고
    • Purification and functional characterization of p16, the ATPase of the bacteriophage phi29 packaging machinary
    • Ibarra B., Valpuesta J.M., Carrascosa J.L. Purification and functional characterization of p16, the ATPase of the bacteriophage phi29 packaging machinary. Nucleic Acids Res. 29:(21):2001;4264-4273.
    • (2001) Nucleic Acids Res. , vol.29 , Issue.21 , pp. 4264-4273
    • Ibarra, B.1    Valpuesta, J.M.2    Carrascosa, J.L.3
  • 21
    • 0036222522 scopus 로고    scopus 로고
    • Myosin IXb is a single-headed minus-end-directed processive motor
    • Inoue A., Saito J., Ikebe R., Ikebe M. Myosin IXb is a single-headed minus-end-directed processive motor. Nat. Cell Biol. 4:2002;302-306.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 302-306
    • Inoue, A.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 22
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III
    • Jeruzalmi D., O'Donnell M., Kuriyan J. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell. 106:2001;429-441.
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 23
    • 0027413261 scopus 로고
    • Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases
    • Koonin E.V., Senkevich V.I., Chernos V.I. Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases. Virus Genes. 7:1993;89-94.
    • (1993) Virus Genes , vol.7 , pp. 89-94
    • Koonin, E.V.1    Senkevich, V.I.2    Chernos, V.I.3
  • 24
    • 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. 69:1995;5018-5023.
    • (1995) J. Virol. , vol.69 , pp. 5018-5023
    • Lee, C.S.1    Guo, P.2
  • 25
    • 0020456350 scopus 로고
    • A bacteriophage T4 DNA packaging related DNA-dependent ATPase-endonuclease
    • Manne V.S., Rao V.B., Black L.W. A bacteriophage T4 DNA packaging related DNA-dependent ATPase-endonuclease. J Biol Chem. 257:1982;13223-13232.
    • (1982) J Biol Chem , vol.257 , pp. 13223-13232
    • Manne, V.S.1    Rao, V.B.2    Black, L.W.3
  • 26
    • 0035043999 scopus 로고    scopus 로고
    • No syringes please, ejection of phage T7 DNA from the virion is enzyme driven
    • Molineux I.J. No syringes please, ejection of phage T7 DNA from the virion is enzyme driven. Mol. Microbiol. 40:2001;1-8.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1-8
    • Molineux, I.J.1
  • 27
    • 0027299633 scopus 로고
    • DNA packaging ATPase of bacteriophage T3
    • Morita M., Tasaka M., Fujisawa H. DNA packaging ATPase of bacteriophage T3. Virology. 193:1993;748-752.
    • (1993) Virology , vol.193 , pp. 748-752
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 28
    • 0015244830 scopus 로고
    • DNA-protein complex in circular DNA from phage φ29
    • Ortin J., Viñuela E., Salas M., Vásquez C. DNA-protein complex in circular DNA from phage φ29. Na. New Biol. 234:1971;275-277.
    • (1971) Na. New Biol. , vol.234 , pp. 275-277
    • Ortin, J.1    Viñuela, E.2    Salas, M.3    Vásquez, C.4
  • 29
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang P.S., Jankowsky E., Planet P.J., Pyle A.M. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J. 21:2002;1168-1176.
    • (2002) EMBO J. , vol.21 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 31
    • 0025358014 scopus 로고
    • Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly
    • Prevelige P.E.J., Thomas D., King J., Towse S.A., Thomas G.J.J. Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly. Biochemistry. 29:1990;5626-5633.
    • (1990) Biochemistry , vol.29 , pp. 5626-5633
    • Prevelige, P.E.J.1    Thomas, D.2    King, J.3    Towse, S.A.4    Thomas, G.J.J.5
  • 32
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome
    • Redenbach M., Kieser H.M., Denapaite D., Eichner A., Cullum J., Kinashi H., Hopwood D.A. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome. Mol. Microbiol. 21:1996;77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 33
    • 0027446475 scopus 로고
    • Chemomechanical cycle of kinesin differs from that of myosin
    • Romberg L., Vale R.D. Chemomechanical cycle of kinesin differs from that of myosin. Nature. 361:1993;168-170.
    • (1993) Nature , vol.361 , pp. 168-170
    • Romberg, L.1    Vale, R.D.2
  • 34
    • 0030894765 scopus 로고    scopus 로고
    • Bipartite structure and functional independence of adenovirus type 5 packaging elements
    • Schmid S.I., Hearing P. Bipartite structure and functional independence of adenovirus type 5 packaging elements. J Virol. 71:1997;3375-3384.
    • (1997) J Virol. , vol.71 , pp. 3375-3384
    • Schmid, S.I.1    Hearing, P.2
  • 35
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • Schnitzer M.J., Block S.M. Kinesin hydrolyses one ATP per 8-nm step. Nature. 388:1997;386-390.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 37
    • 0026600963 scopus 로고
    • Bacteriophage P1 genes involved in the recognition and cleavage of the phage packaging site (pac)
    • Skorupski K., Pierce J.C., Sauer B., Sternberg N. Bacteriophage P1 genes involved in the recognition and cleavage of the phage packaging site (pac). J. Mol. Biol. 223:1992;977-989.
    • (1992) J. Mol. Biol. , vol.223 , pp. 977-989
    • Skorupski, K.1    Pierce, J.C.2    Sauer, B.3    Sternberg, N.4
  • 38
    • 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. 413:2001;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
  • 39
    • 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. 71:1997;487-494.
    • (1997) J. Virol. , vol.71 , pp. 487-494
    • Trottier, M.1    Guo, P.2
  • 40
    • 0030602794 scopus 로고    scopus 로고
    • DNA helicases: New breeds of translocating motors and molecular pumps
    • West S.C. DNA helicases new breeds of translocating motors and molecular pumps . Cell. 86:1996;177-180.
    • (1996) Cell , vol.86 , pp. 177-180
    • West, S.C.1
  • 41
    • 0032531835 scopus 로고    scopus 로고
    • Regulated processive transcription of chromatin by T7 RNA polymerase in Trypanosoma brucei
    • Wirtz E., Hoek M., Cross G.A. Regulated processive transcription of chromatin by T7 RNA polymerase in Trypanosoma brucei. Nucleic Acids Res. 26:1998;4626-4634.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4626-4634
    • Wirtz, E.1    Hoek, M.2    Cross, G.A.3
  • 42
    • 0017595501 scopus 로고
    • Studies related to the head-maturation pathway of bacteriophages T4 and T2. I. morphology and kinetics of intracellular particles produced by mutants in the maturation genes
    • Wunderli H., vd B.J., Kellenberger E. Studies related to the head-maturation pathway of bacteriophages T4 and T2. I. morphology and kinetics of intracellular particles produced by mutants in the maturation genes. J Supramol. Struct. 7:1977;135-161.
    • (1977) J Supramol. Struct. , vol.7 , pp. 135-161
    • Wunderli, H.1    Vd, B.J.2    Kellenberger, E.3
  • 43
    • 0022447747 scopus 로고
    • Cloning and sequencing of the genetic right end of bacteriophage T3 DNA
    • Yamada M., Fujisawa H., Kato H., Hamada K., Minagawa T. Cloning and sequencing of the genetic right end of bacteriophage T3 DNA. Virology. 151:1986;350-361.
    • (1986) Virology , vol.151 , pp. 350-361
    • Yamada, M.1    Fujisawa, H.2    Kato, H.3    Hamada, K.4    Minagawa, T.5
  • 44
    • 0028870215 scopus 로고
    • Specific interaction of terminase, the DNA packaging enzyme of bacteriophage lambda, with the portal protein of the prohead
    • Yeo A., Feiss M. Specific interaction of terminase, the DNA packaging enzyme of bacteriophage lambda, with the portal protein of the prohead. J.Mol.Biol. 245:1995;141-150.
    • (1995) J.Mol.Biol. , vol.245 , pp. 141-150
    • Yeo, A.1    Feiss, M.2
  • 45
    • 0032579608 scopus 로고    scopus 로고
    • Generic analysis of the UL15 gene locus for the putative terminase of herpes simplex virus type 1
    • Yu D., Weller S.K. Generic analysis of the UL15 gene locus for the putative terminase of herpes simplex virus type 1. Virology. 243:1998;32-44.
    • (1998) Virology , vol.243 , pp. 32-44
    • Yu, D.1    Weller, S.K.2
  • 46
    • 0028361637 scopus 로고
    • The proximate 5′ and 3′ ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage φ29 DNA
    • Zhang C.L., Lee C.-S., Guo P. The proximate 5′ and 3′ ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage φ29 DNA. Virology. 201:1994;77-85.
    • (1994) Virology , vol.201 , pp. 77-85
    • Zhang, C.L.1    Lee, C.-S.2    Guo, P.3
  • 48
    • 0034795897 scopus 로고    scopus 로고
    • Role for the adenovirus IVa2 protein in packaging of viral DNA
    • Zhang W., Low J.A., Christensen J.B., Imperiale M.J. Role for the adenovirus IVa2 protein in packaging of viral DNA. J. Virol. 75:2001;10446-10454.
    • (2001) J. Virol. , vol.75 , pp. 10446-10454
    • Zhang, W.1    Low, J.A.2    Christensen, J.B.3    Imperiale, M.J.4


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