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Volumn 726, Issue , 2012, Pages 489-509

The bacteriophage DNA packaging machine

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIOPHAGE DNA; CAPSID PROTEIN; ENDONUCLEASE; MOLECULAR MOTOR; NUCLEASE; VIRUS DNA;

EID: 84858273215     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-0980-9_22     Document Type: Article
Times cited : (106)

References (100)
  • 3
    • 69949139694 scopus 로고    scopus 로고
    • The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor
    • Al-Zahrani AS, Kondabagil K, Gao S, Kelly N, Ghosh-Kumar M, Rao VB (2009) The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor. J Biol Chem 284:24490-24500
    • (2009) J Biol Chem , vol.284 , pp. 24490-24500
    • Al-Zahrani, A.S.1    Kondabagil, K.2    Gao, S.3    Kelly, N.4    Ghosh-Kumar, M.5    Rao, V.B.6
  • 4
    • 0032902757 scopus 로고    scopus 로고
    • Mutations that extend the specificity of the endonuclease activity of λ terminase
    • Arens JS, Hang Q, Hwang Y, Tuma B, Max S (1999) Mutations that extend the specifi city of the endonuclease activity of lambda terminase. J Bacteriol 181:218-224 (Pubitemid 29013674)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 218-224
    • Arens, J.S.1    Hang, Q.2    Hwang, Y.3    Tuma, B.4    Max, S.5    Feiss, M.6
  • 5
    • 33745190954 scopus 로고    scopus 로고
    • Portal fusion protein constraints on function in DNA packaging of bacteriophage T4
    • Baumann RG, Mullaney J, Black LW (2006) Portal fusion protein constraints on function in DNA packaging of bacteriophage T4. Mol Microbiol 61:16-32
    • (2006) Mol Microbiol , vol.61 , pp. 16-32
    • Baumann, R.G.1    Mullaney, J.2    Black, L.W.3
  • 6
    • 0002107186 scopus 로고
    • Control mechanisms in dsDNA bacteriophage assembly
    • Calendar R (ed) 1st edn. Plenum, New York
    • Casjens S, Hendrix R (1988) Control mechanisms in dsDNA bacteriophage assembly. In: Calendar R (ed) The bacteriophages, 1st edn. Plenum, New York, pp 15-91
    • (1988) The Bacteriophages , pp. 15-91
    • Casjens, S.1    Hendrix, R.2
  • 7
    • 0023234299 scopus 로고
    • Initiation of bacteriophage P22 DNA packaging series. Analysis of a mutant that alters the DNA target specificity of the packaging apparatus
    • DOI 10.1016/0022-2836(87)90671-1
    • Casjens S, Huang WM, Hayden M, Parr R (1987) Initiation of bacteriophage P22 DNA packaging series. Analysis of a mutant that alters the DNA target specifi city of the packaging apparatus. J Mol Biol 194:411-422 (Pubitemid 17081565)
    • (1987) Journal of Molecular Biology , vol.194 , Issue.3 , pp. 411-422
    • Casjens, S.1    Huang, W.M.2    Hayden, M.3    Parr, R.4
  • 8
    • 0026474362 scopus 로고
    • Molecular genetic analysis of bacteriophage P22 gene 3 product, a protein involved in the initiation of headful DNA packaging
    • Casjens S, Sampson L, Randall S, Eppler K, Wu H, Petri JB, Schmieger H (1992a) Molecular genetic analysis of bacteriophage P22 gene 3 product, a protein involved in the initiation of headful DNA packaging. J Mol Biol 227:1086-1099
    • (1992) J Mol Biol , vol.227 , pp. 1086-1099
    • Casjens, S.1    Sampson, L.2    Randall, S.3    Eppler, K.4    Wu, H.5    Petri, J.B.6    Schmieger, H.7
  • 10
    • 0029129145 scopus 로고
    • Virus DNA packaging: The strategy used by phage lambda
    • Catalano CE, Cue D, Feiss M (1995) Virus DNA packaging: the strategy used by phage lambda. Mol Microbiol 16:1075-1086
    • (1995) Mol Microbiol , vol.16 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 11
    • 0029093926 scopus 로고
    • The small subunit of the terminase enzyme of Bacillus subtilis bacteriophage SPP1 forms a specialized nucleoprotein complex with the packaging initiation region
    • Chai S, Lurz R, Alonso JC (1995) The small subunit of the terminase enzyme of Bacillus subtilis bacteriophage SPP1 forms a specialized nucleoprotein complex with the packaging initiation region. J Mol Biol 252:386-398
    • (1995) J Mol Biol , vol.252 , pp. 386-398
    • Chai, S.1    Lurz, R.2    Alonso, J.C.3
  • 12
    • 0016168104 scopus 로고
    • Location of DNA ends in P2, 186, P4 and lambda bacteriophage heads
    • Chattoraj DK, Inman RB (1974) Location of DNA ends in P2, 186, P4 and lambda bacteriophage heads. J Mol Biol 87:11-22
    • (1974) J Mol Biol , vol.87 , pp. 11-22
    • Chattoraj, D.K.1    Inman, R.B.2
  • 13
    • 38649114349 scopus 로고    scopus 로고
    • Three-dimensional architecture of the bacteriophage φ29 packaged genome and elucidation of its packaging process
    • DOI 10.1016/j.virol.2007.07.035, PII S0042682207004990
    • Comolli LR, Spakowitz AJ, Siegerist CE, Jardine PJ, Grimes S, Anderson DL, Bustamante C, Downing KH (2008) Three-dimensional architecture of the bacteriophage phi29 packaged genome and elucidation of its packaging process. Virology 371:267-277 (Pubitemid 351173222)
    • (2008) Virology , vol.371 , Issue.2 , pp. 267-277
    • Comolli, L.R.1    Spakowitz, A.J.2    Siegerist, C.E.3    Jardine, P.J.4    Grimes, S.5    Anderson, D.L.6    Bustamante, C.7    Downing, K.H.8
  • 14
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • DOI 10.1038/sj.emboj.7600272
    • Cordin O, Tanner NK, Doere M, Linder P, Banroques J (2004) The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J 23:2478-2487 (Pubitemid 38988220)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 15
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • DOI 10.1016/j.gene.2005.10.019, PII S0378111905006359
    • Cordin O, Banroques J, Tanner NK, Linder P (2006) The DEAD-box protein family of RNA helicases. Gene 367:17-37 (Pubitemid 43286737)
    • (2006) Gene , vol.367 , Issue.1-2 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 16
    • 0000000628 scopus 로고
    • Mutations abolishing the endonuclease activity of bacteriophage lambda terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA binding domain
    • Davidson A, Gold M (1992) Mutations abolishing the endonuclease activity of bacteriophage lambda terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA binding domain. Virology 161:305-315
    • (1992) Virology , vol.161 , pp. 305-315
    • Davidson, A.1    Gold, M.2
  • 17
    • 0034279457 scopus 로고    scopus 로고
    • Assignment of the 1H, 13C, and 15N resonances of the DNA binding domain of gpNu1, a genome packaging protein from bacteriophage lambda
    • de Beer T, Ortega M, Berton N, Yang Q, Overduin M, Catalano CE (2000) Assignment of the 1H, 13C, and 15N resonances of the DNA binding domain of gpNu1, a genome packaging protein from bacteriophage lambda. J Biomol NMR 18:69-70
    • (2000) J Biomol NMR , vol.18 , pp. 69-70
    • De Beer, T.1    Ortega, M.2    Berton, N.3    Yang, Q.4    Overduin, M.5    Catalano, C.E.6
  • 19
    • 14144256682 scopus 로고    scopus 로고
    • Bacteriophage λ terminase: Alterations of the high-affinity ATPase affect viral DNA packaging
    • DOI 10.1016/j.jmb.2004.12.041
    • Dhar A, Feiss M (2005) Bacteriophage lambda terminase: alterations of the high-affi nity ATPase affect viral DNA packaging. J Mol Biol 347:71-80 (Pubitemid 40283629)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.1 , pp. 71-80
    • Dhar, A.1    Feiss, M.2
  • 21
    • 34247368838 scopus 로고    scopus 로고
    • An ATP Hydrolysis Sensor in the DNA Packaging Motor from Bacteriophage T4 Suggests an Inchworm-Type Translocation Mechanism
    • DOI 10.1016/j.jmb.2007.03.019, PII S0022283607003439
    • Draper B, Rao VB (2007) An ATP hydrolysis sensor in the DNA packaging motor from bacteriophage T4 suggests an inchworm-type translocation mechanism. J Mol Biol 369:79-94 (Pubitemid 46635439)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.1 , pp. 79-94
    • Draper, B.1    Rao, V.B.2
  • 22
    • 0036300304 scopus 로고    scopus 로고
    • The large subunit of bacteriophage λ's terminase plays a role in DNA translocation and packaging termination
    • DOI 10.1006/jmbi.2001.5368
    • Duffy C, Feiss M (2002) The large subunit of bacteriophage lambda's terminase plays a role in DNA translocation and packaging termination. J Mol Biol 316:547-561 (Pubitemid 34729240)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.3 , pp. 547-561
    • Duffy, C.1    Feiss, M.2
  • 23
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw WC, Casjens SR (1980) DNA packaging by the double-stranded DNA bacteriophages. Cell 21:319-331 (Pubitemid 10047085)
    • (1980) Cell , vol.21 , Issue.2 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 25
    • 0016702694 scopus 로고
    • Polarized packaging of bacteriophage lambda chromosomes
    • Feiss M, Bublitz A (1975) Polarized packaging of bacteriophage lambda chromosomes. J Mol Biol 94:583-594
    • (1975) J Mol Biol , vol.94 , pp. 583-594
    • Feiss, M.1    Bublitz, A.2
  • 26
    • 74249110550 scopus 로고    scopus 로고
    • DNA packaging by lambda-like bacteriophages: Mutations broadening the packaging specifi city of terminase, the lambda-packaging enzyme
    • Feiss M, Reynolds E, Schrock M, Sippy J (2010) DNA packaging by lambda-like bacteriophages: mutations broadening the packaging specifi city of terminase, the lambda-packaging enzyme. Genetics 184:43-52
    • (2010) Genetics , vol.184 , pp. 43-52
    • Feiss, M.1    Reynolds, E.2    Schrock, M.3    Sippy, J.4
  • 27
    • 0022432143 scopus 로고
    • The terminase of bacteriophage lambda. Functional domains for cosB binding and multimer assembly
    • Frackman S, Siegele DA, Feiss M (1985) The terminase of bacteriophage lambda. Functional domains for cosB binding and multimer assembly. J Mol Biol 183:225-238
    • (1985) J Mol Biol , vol.183 , pp. 225-238
    • Frackman, S.1    Siegele, D.A.2    Feiss, M.3
  • 28
    • 0031218420 scopus 로고    scopus 로고
    • Phage DNA packaging
    • Fujisawa H, Morita M (1997) Phage DNA packaging. Genes Cells 2:537-545 (Pubitemid 127688601)
    • (1997) Genes to Cells , vol.2 , Issue.9 , pp. 537-545
    • Fujisawa, H.1    Morita, M.2
  • 30
    • 35148815738 scopus 로고    scopus 로고
    • Measurements of Single DNA Molecule Packaging Dynamics in Bacteriophage λ Reveal High Forces, High Motor Processivity, and Capsid Transformations
    • DOI 10.1016/j.jmb.2007.09.011, PII S0022283607011850
    • Fuller DN, Raymer DM, Rickgauer JP, Robertson RM, Catalano CE, Anderson DL, Grimes S, Smith DE (2007b) Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations. J Mol Biol 373:1113-1122 (Pubitemid 47542509)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1113-1122
    • Fuller, D.N.1    Raymer, D.M.2    Rickgauer, J.P.3    Robertson, R.M.4    Catalano, C.E.5    Anderson, D.L.6    Grimes, S.7    Smith, D.E.8
  • 31
    • 79952802006 scopus 로고    scopus 로고
    • Specificity of interactions among the DNA-packaging machine components of T4-related bacteriophages
    • Gao S, Rao VB (2011) Specifi city of interactions among the DNA-packaging machine components of T4-related bacteriophages. J Biol Chem 286:3944-3956
    • (2011) J Biol Chem , vol.286 , pp. 3944-3956
    • Gao, S.1    Rao, V.B.2
  • 32
    • 79954570731 scopus 로고    scopus 로고
    • Regulation by interdomain communication of a headful packaging nuclease from bacteriophage T4
    • Ghosh-Kumar M, Alam TI, Draper B, Stack JD, Rao VB (2011) Regulation by interdomain communication of a headful packaging nuclease from bacteriophage T4. Nucleic Acids Res 39:2742-2755
    • (2011) Nucleic Acids Res , vol.39 , pp. 2742-2755
    • Ghosh-Kumar, M.1    Alam, T.I.2    Draper, B.3    Stack, J.D.4    Rao, V.B.5
  • 33
    • 0038499685 scopus 로고    scopus 로고
    • Defining the ATPase center of bacteriophage T4 DNA packaging machine: Requirement for a catalytic glutamate residue in the large terminase protein gp17
    • DOI 10.1016/S0022-2836(03)00636-3
    • Goetzinger K, Rao V (2003) Defi ning the ATPase center of bacteriophage T4 DNA packaging machine: requirement for a catalytic glutamate residue in the large terminase protein gp17. J Mol Biol 331:139-154 (Pubitemid 36870782)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.1 , pp. 139-154
    • Goetzinger, K.R.1    Rao, V.B.2
  • 35
    • 79958703404 scopus 로고    scopus 로고
    • Role of the '29 connector channel loops in late-stage DNA packaging
    • Grimes S, Ma, S, Gao J, Atz R, Jardine P (2011) Role of the '29 connector channel loops in late-stage DNA packaging. J Mol Biol 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.5
  • 36
    • 0032520542 scopus 로고    scopus 로고
    • Characterization of the small subunit of the terminase enzyme of the Bacillus subtilis bacteriophage SPP1
    • DOI 10.1006/viro.1997.9017
    • Gual A, Alonso JC (1998) Characterization of the small subunit of the terminase enzyme of the Bacillus subtilis bacteriophage SPP1. Virology 242:279-287 (Pubitemid 28414733)
    • (1998) Virology , vol.242 , Issue.2 , pp. 279-287
    • Gual, A.1    Alonso, J.C.2
  • 38
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage Φ29 DNA
    • Guo PX, Erickson S, Anderson D (1987) A small viral RNA is required for in vitro packaging of bacteriophage phi 29 DNA. Science (New York, NY) 236:690-694 (Pubitemid 17076855)
    • (1987) Science , vol.236 , Issue.4802 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 39
    • 0034730389 scopus 로고    scopus 로고
    • An ATPase center of bacteriophage lambda terminase involved in post-cleavage stages of DNA packaging: Identifi cation of ATP-interactive amino acids
    • Hang Q, Tack B, Feiss M (2000) An ATPase center of bacteriophage lambda terminase involved in post-cleavage stages of DNA packaging: identifi cation of ATP-interactive amino acids. J Mol Biol 302:777-795
    • (2000) J Mol Biol , vol.302 , pp. 777-795
    • Hang, Q.1    Tack, B.2    Feiss, M.3
  • 40
    • 79953887810 scopus 로고    scopus 로고
    • The Prohead-I structure of bacteriophage HK97: Implications for scaffold-mediated control of particle assembly and maturation
    • Huang RK, Khayat R, Lee KK, Gertsman I, Duda RL, Hendrix RW, Johnson JE (2011) The Prohead-I structure of bacteriophage HK97: implications for scaffold-mediated control of particle assembly and maturation. J Mol Biol 408:541-554
    • (2011) J Mol Biol , vol.408 , pp. 541-554
    • Huang, R.K.1    Khayat, R.2    Lee, K.K.3    Gertsman, I.4    Duda, R.L.5    Hendrix, R.W.6    Johnson, J.E.7
  • 41
    • 0030606851 scopus 로고    scopus 로고
    • Mutations affecting the high affinity ATPase center of gpA, the large subunit of bacteriophage λ terminase, inactivate the endonuclease activity of terminase
    • DOI 10.1006/jmbi.1996.0480
    • Hwang Y, Feiss M (1996) Mutations affecting the high affi nity ATPase center of gpA, the large subunit of bacteriophage lambda terminase, inactivate the endonuclease activity of terminase. J Mol Biol 261:524-535 (Pubitemid 26335944)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.4 , pp. 524-535
    • Hwang, Y.1    Feiss, M.2
  • 42
    • 0034634309 scopus 로고    scopus 로고
    • The endonuclease and helicase activities of bacteriophage lambda terminase: Changing nearby residue 515 restores activity to the gpA K497D mutant enzyme
    • Hwang Y, Feiss M (2000) The endonuclease and helicase activities of bacteriophage lambda terminase: changing nearby residue 515 restores activity to the gpA K497D mutant enzyme. Virology 277:204-214
    • (2000) Virology , vol.277 , pp. 204-214
    • Hwang, Y.1    Feiss, M.2
  • 43
    • 1942521214 scopus 로고    scopus 로고
    • The portal protein plays essential roles at different steps of the SPP1 DNA packaging process
    • DOI 10.1016/j.virol.2004.02.012, PII S0042682204001217
    • Isidro A, Henriques AO, Tavares P (2004a) The portal protein plays essential roles at different steps of the SPP1 DNA packaging process. Virology 322:253-263 (Pubitemid 38521140)
    • (2004) Virology , vol.322 , Issue.2 , pp. 253-263
    • Isidro, A.1    Henriques, A.O.2    Tavares, P.3
  • 44
    • 1442276352 scopus 로고    scopus 로고
    • The high-resolution functional map of bacteriophage SPP1 portal protein
    • DOI 10.1046/j.1365-2958.2003.03880.x
    • Isidro A, Santos MA, Henriques AO, Tavares P (2004b) The high-resolution functional map of bacteriophage SPP1 portal protein. Mol Microbiol 51:949-962 (Pubitemid 38270791)
    • (2004) Molecular Microbiology , vol.51 , Issue.4 , pp. 949-962
    • Isidro, A.1    Santos, M.A.2    Henriques, A.O.3    Tavares, P.4
  • 45
    • 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
    • DOI 10.1093/nar/gkh828
    • Iyer LM, Makarova KS, Koonin EV, Aravind L (2004) 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 32:5260-5279 (Pubitemid 39445514)
    • (2004) Nucleic Acids Research , vol.32 , Issue.17 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 46
    • 77956448643 scopus 로고    scopus 로고
    • One-way traffi c of a viral motor channel for double-stranded DNA translocation
    • Jing P, Haque F, Shu D, Guo P (2010) One-way traffi c of a viral motor channel for double-stranded DNA translocation. Nano Lett 10(9):3620-3627
    • (2010) Nano Lett , vol.10 , Issue.9 , pp. 3620-3627
    • Jing, P.1    Haque, F.2    Shu, D.3    Guo, P.4
  • 47
    • 34147123766 scopus 로고    scopus 로고
    • DNA packaging and delivery machines in tailed bacteriophages
    • DOI 10.1016/j.sbi.2007.03.011, PII S0959440X07000413, Theory and Simulation / Mecromolecular Assemblages
    • Johnson JE, Chiu W (2007) DNA packaging and delivery machines in tailed bacteriophages. Curr Opin Struct Biol 17:237-243 (Pubitemid 46575256)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.2 , pp. 237-243
    • Johnson, J.E.1    Chiu, W.2
  • 49
    • 0024511425 scopus 로고
    • Structure and inherent properties of the bacteriophage lambda head shell. VI. DNA-packaging-defective mutants in the major capsid protein
    • DOI 10.1016/0022-2836(89)90350-1
    • Katsura I (1989) Structure and inherent properties of the bacteriophage lambda head shell. VI. DNA-packagingdefective mutants in the major capsid protein. J Mol Biol 205:397-405 (Pubitemid 19060192)
    • (1989) Journal of Molecular Biology , vol.205 , Issue.2 , pp. 397-405
    • Katsura, I.1
  • 50
    • 33645101691 scopus 로고    scopus 로고
    • A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: Insights into DNA packaging initiation and assembly of packaging motor
    • Kondabagil KR, Rao VB (2006) A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: insights into DNA packaging initiation and assembly of packaging motor. J Mol Biol 358:67-82
    • (2006) J Mol Biol , vol.358 , pp. 67-82
    • Kondabagil, K.R.1    Rao, V.B.2
  • 51
    • 0032483313 scopus 로고    scopus 로고
    • Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4
    • DOI 10.1006/jmbi.1998.1952
    • Kuebler D, Rao VB (1998) Functional analysis of the DNA-packaging/ terminase protein gp17 from bacteriophage T4. J Mol Biol 281:803-814 (Pubitemid 28408430)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.5 , pp. 803-814
    • Kuebler, D.1    Rao, V.B.2
  • 55
    • 0032030444 scopus 로고    scopus 로고
    • DNA requirements in vivo for phage T4 packaging
    • DOI 10.1006/viro.1997.9019
    • Lin H, Black LW (1998) DNA requirements in vivo for phage T4 packaging. Virology 242:118-127 (Pubitemid 28396365)
    • (1998) Virology , vol.242 , Issue.1 , pp. 118-127
    • Lin, H.1    Black, L.W.2
  • 56
    • 0031023655 scopus 로고    scopus 로고
    • Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging
    • DOI 10.1074/jbc.272.6.3495
    • Lin H, Simon MN, Black LW (1997) Purifi cation and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging. J Biol Chem 272:3495-3501 (Pubitemid 27066850)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3495-3501
    • Lin Hsingchi1    Simon, M.N.2    Black, L.W.3
  • 57
    • 14744306883 scopus 로고    scopus 로고
    • Self-association properties of the bacteriophage λ terminase holoenzyme: Implications for the DNA packaging motor
    • DOI 10.1016/j.jmb.2005.01.016
    • Maluf N, Yang Q, Catalano C (2005) Self-association properties of the bacteriophage lambda terminase holoenzyme: implications for the DNA packaging motor. J Mol Biol 347:523-542 (Pubitemid 40332362)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.3 , pp. 523-542
    • Maluf, N.K.1    Yang, Q.2    Catalano, C.E.3
  • 58
    • 33845947499 scopus 로고    scopus 로고
    • Assembly of bacteriophage lambda terminase into a viral DNA maturation and packaging machine
    • DOI 10.1021/bi0615036
    • Maluf N, Gaussier H, Bogner E, Feiss M, Catalano C (2006) Assembly of bacteriophage lambda terminase into a viral DNA maturation and packaging machine. Biochemistry 45:15259-15268 (Pubitemid 46032453)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15259-15268
    • Maluf, N.K.1    Gaussier, H.2    Bogner, E.3    Feiss, M.4    Catalano, C.E.5
  • 59
    • 1642487764 scopus 로고    scopus 로고
    • Novel and deviant Walker A ATP-binding motifs in bacteriophage large terminase-DNA packaging proteins
    • DOI 10.1016/j.virol.2003.11.006, PII S0042682203008365
    • Mitchell MS, Rao VB (2004) Novel and deviant Walker A ATP-binding motifs in bacteriophage large terminase-DNA packaging proteins. Virology 321:217-221 (Pubitemid 38406036)
    • (2004) Virology , vol.321 , Issue.2 , pp. 217-221
    • Mitchell, M.S.1    Rao, V.B.2
  • 60
    • 33644850527 scopus 로고    scopus 로고
    • Functional analysis of the bacteriophage T4 DNA-packaging ATPase motor
    • DOI 10.1074/jbc.M507719200
    • Mitchell MS, Rao VB (2006) Functional analysis of the bacteriophage T4 DNA-packaging ATPase motor. J Biol Chem 281:518-527 (Pubitemid 43671215)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 518-527
    • Mitchell, M.S.1    Rao, V.B.2
  • 61
    • 0037106323 scopus 로고    scopus 로고
    • Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases
    • Mitchell M, Matsuzaki S, Imai S, Rao V (2002) Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Res 30:4009-4021
    • (2002) Nucleic Acids Res , vol.30 , pp. 4009-4021
    • Mitchell, M.1    Matsuzaki, S.2    Imai, S.3    Rao, V.4
  • 62
    • 22044451059 scopus 로고    scopus 로고
    • Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29
    • DOI 10.1016/j.jmb.2005.05.038, PII S0022283605005814
    • Moll WD, Guo P (2005) Translocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29. J Mol Biol 351:100-107 (Pubitemid 40967058)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.1 , pp. 100-107
    • Moll, W.-D.1    Guo, P.2
  • 64
    • 0027299633 scopus 로고
    • DNA packaging ATPase of bacteriophage T3
    • Morita M, Tasaka M, Fujisawa H (1993) DNA packaging ATPase of bacteriophage T3. Virology 193:748-752
    • (1993) Virology , vol.193 , pp. 748-752
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 66
    • 35548950227 scopus 로고    scopus 로고
    • Subunit Conformations and Assembly States of a DNA-translocating Motor: The Terminase of Bacteriophage P22
    • DOI 10.1016/j.jmb.2007.08.070, PII S0022283607012302
    • Nemecek D, Gilcrease EB, Kang S, Preveilige PE Jr, Casjens S, Thomas GJ Jr (2007) Subunit conformations and assembly states of a DNA-translocating motor: the terminase of bacteriophage P22. J Mol Biol 374:817-836 (Pubitemid 350018767)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.3 , pp. 817-836
    • Nemecek, D.1    Gilcrease, E.B.2    Kang, S.3    Prevelige Jr., P.E.4    Casjens, S.5    Thomas Jr., G.J.6
  • 68
    • 33646004109 scopus 로고    scopus 로고
    • Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release
    • Nowotny M, Yang W (2006) Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release. EMBO J 25:1924-1933
    • (2006) EMBO J , vol.25 , pp. 1924-1933
    • Nowotny, M.1    Yang, W.2
  • 71
    • 77951245717 scopus 로고    scopus 로고
    • Direct interaction of the bacteriophage SPP1 packaging ATPase with the portal protein
    • Oliveira L, Cuervo A, Tavares P (2010) Direct interaction of the bacteriophage SPP1 packaging ATPase with the portal protein. J Biol Chem 285:7366-7373
    • (2010) J Biol Chem , vol.285 , pp. 7366-7373
    • Oliveira, L.1    Cuervo, A.2    Tavares, P.3
  • 72
    • 46649088725 scopus 로고    scopus 로고
    • Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure
    • Oram M, Sabanayagam C, Black LW (2008) Modulation of the packaging reaction of bacteriophage T4 terminase by DNA structure. J Mol Biol 381:61-72
    • (2008) J Mol Biol , vol.381 , pp. 61-72
    • Oram, M.1    Sabanayagam, C.2    Black, L.W.3
  • 74
    • 34848897808 scopus 로고    scopus 로고
    • The DNA Maturation Domain of gpA, the DNA Packaging Motor Protein of Bacteriophage Lambda, Contains an ATPase Site Associated with Endonuclease Activity
    • DOI 10.1016/j.jmb.2007.07.067, PII S0022283607010327
    • Ortega ME, Gaussier H, Catalano CE (2007) The DNA maturation domain of gpA, the DNA packaging motor protein of bacteriophage lambda, contains an ATPase site associated with endonuclease activity. J Mol Biol 373:851-865 (Pubitemid 47498432)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.4 , pp. 851-865
    • Ortega, M.E.1    Gaussier, H.2    Catalano, C.E.3
  • 75
    • 33646851613 scopus 로고    scopus 로고
    • The endonuclease domain of bacteriophage terminases belongs to the resolvase/integrase/ribonuclease H superfamily: A bioinformatics analysis validated by a functional study on bacteriophage T5
    • DOI 10.1074/jbc.M511817200
    • Ponchon L, Boulanger P, Labesse G, Letellier L (2006) The endonuclease domain of bacteriophage terminases belongs to the resolvase/integrase/ ribonuclease H superfamily: a bioinformatics analysis validated by a functional study on bacteriophage T5. J Biol Chem 281:5829-5836 (Pubitemid 43847682)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5829-5836
    • Ponchon, L.1    Boulanger, P.2    Labesse, G.3    Letellier, L.4
  • 76
    • 78651293238 scopus 로고    scopus 로고
    • Salt-Dependent DNA-DNA Spacings in Intact Bacteriophage lambda Refl ect Relative Importance of DNA Self-Repulsion and Bending Energies
    • Qiu X, Rau DC, Parsegian VA, Fang LT, Knobler CM, Gelbart WM (2011) Salt-Dependent DNA-DNA Spacings in Intact Bacteriophage lambda Refl ect Relative Importance of DNA Self-Repulsion and Bending Energies. Phys Rev Lett 106:028102
    • (2011) Phys Rev Lett , vol.106 , pp. 028102
    • Qiu, X.1    Rau, D.C.2    Parsegian, V.A.3    Fang, L.T.4    Knobler, C.M.5    Gelbart, W.M.6
  • 77
    • 0021968411 scopus 로고
    • DNA packaging of bacteriophage T4 proheads in vitro evidence that prohead expansion is not coupled to DNA packaging
    • DOI 10.1016/0022-2836(85)90072-5
    • Rao VB, Black LW (1985) DNA packaging of bacteriophage T4 proheads in vitro. Evidence that prohead expansion is not coupled to DNA packaging. J Mol Biol 185:565-578 (Pubitemid 15241165)
    • (1985) Journal of Molecular Biology , vol.185 , Issue.3 , pp. 565-578
    • Rao, V.B.1    Black, L.W.2
  • 79
    • 75849131151 scopus 로고    scopus 로고
    • DNA crunching by a viral packaging motor: Compression of a procapsid-portal stalled Y-DNA substrate
    • Ray K, Sabanayagam CR, Lakowicz JR, Black LW (2010) DNA crunching by a viral packaging motor: compression of a procapsid-portal stalled Y-DNA substrate. Virology 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
  • 80
    • 0142226893 scopus 로고    scopus 로고
    • Defining the bacteriophage T4 DNA packaging machine: Evidence for a C-terminal DNA cleavage domain in the large terminase/packaging protein gp17
    • DOI 10.1016/j.jmb.2003.09.028
    • Rentas FJ, Rao VB (2003) Defi ning the bacteriophage T4 DNA packaging machine: evidence for a C-terminal DNA cleavage domain in the large terminase/packaging protein gp17. J Mol Biol 334:37-52 (Pubitemid 37330098)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.1 , pp. 37-52
    • Rentas, F.J.1    Rao, V.B.2
  • 81
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250:194-199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 82
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system
    • DOI 10.1038/sj.emboj.7601506, PII 7601506
    • Shu D, Zhang H, Jin J, Guo P (2007) Counting of six pRNAs of phi29 DNA-packaging motor with customized singlemolecule dual-view system. EMBO J 26:527-537 (Pubitemid 46160952)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 84
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage φ29 portal motor can package DNA against a large internal force
    • DOI 10.1038/35099581
    • Smith D, Tans S, Smith S, Grimes S, Anderson D, Bustamante C (2001) The bacteriophage straight phi29 portal motor can package DNA against a large internal force. Nature 413:748-752 (Pubitemid 33009954)
    • (2001) Nature , vol.413 , Issue.6857 , 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
  • 86
    • 0017596750 scopus 로고
    • Packaging of coliphage lambda DNA. II. The role of the gene D protein
    • Sternberg N, Weisberg R (1977) Packaging of coliphage lambda DNA. II. The role of the gene D protein. J Mol Biol 117:733-759 (Pubitemid 8256701)
    • (1977) Journal of Molecular Biology , vol.117 , Issue.3 , pp. 733-759
    • Sternberg, N.1    Weisberg, R.2
  • 87
    • 33947281384 scopus 로고    scopus 로고
    • The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids
    • DOI 10.1016/j.molcel.2007.02.013, PII S109727650700113X
    • Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB (2007) The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol Cell 25:943-949 (Pubitemid 46436529)
    • (2007) Molecular Cell , vol.25 , Issue.6 , pp. 943-949
    • Sun, S.1    Kondabagil, K.2    Gentz, P.M.3    Rossmann, M.G.4    Rao, V.B.5
  • 90
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • DOI 10.1016/S1097-2765(03)00006-6
    • Tanner NK, Cordin O, Banroques J, Doere M, Linder P (2003) The Q motif: a newly identifi ed motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol Cell 11:127-138 (Pubitemid 36126596)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 91
    • 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 JM, Sippy J, Feiss M, Smith DE (2009) The Q motif of a viral packaging motor governs its force generation and communicates ATP recognition to DNA interaction. Proc Natl Acad Sci USA 106:14355-14360
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14355-14360
    • Tsay, J.M.1    Sippy, J.2    Feiss, M.3    Smith, D.E.4
  • 92
    • 77954903255 scopus 로고    scopus 로고
    • Mutations altering a structurally conserved loop-helix-loop region of a viral packaging motor change DNA translocation velocity and processivity
    • Tsay JM, Sippy J, Deltoro D, Andrews BT, Draper B, Rao V, Catalano CE, Feiss M, Smith DE (2010) Mutations altering a structurally conserved loop-helix-loop region of a viral packaging motor change DNA translocation velocity and processivity. J Biol Chem 285(31):24282-24289
    • (2010) J Biol Chem , vol.285 , Issue.31 , pp. 24282-24289
    • Tsay, J.M.1    Sippy, J.2    Deltoro, D.3    Andrews, B.T.4    Draper, B.5    Rao, V.6    Catalano, C.E.7    Feiss, M.8    Smith, D.E.9
  • 93
    • 3242673586 scopus 로고    scopus 로고
    • 2+-dependent virus, λ shp
    • DOI 10.1016/j.virol.2004.05.024, PII S0042682204003861
    • Wendt J, Feiss M (2004) A fragile lattice: replacing bacteriophage l's head stability gene D with the shp gene of phage 21 generates the Mg ++ -dependent virus, lambda shp . Virology 326:41-46 (Pubitemid 38943004)
    • (2004) Virology , vol.326 , Issue.1 , pp. 41-46
    • Wendt, J.L.1    Feiss, M.2
  • 94
    • 0036034939 scopus 로고    scopus 로고
    • The DNA site utilized by bacteriophage P22 for initiation of DNA packaging
    • DOI 10.1046/j.1365-2958.2002.03114.x
    • Wu H, Sampson L, Parr R, Casjens S (2002) The DNA site utilized by bacteriophage P22 for initiation of DNA packaging. Mol Microbiol 45:1631-1646 (Pubitemid 35231979)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1631-1646
    • Wu, H.1    Sampson, L.2    Parr, R.3    Casjens, S.4
  • 95
    • 37349102695 scopus 로고    scopus 로고
    • L28 at the nonpermissive temperature
    • DOI 10.1128/JVI.01875-07
    • Yang K, Poon AP, Roizman B, Baines JD (2008a) Temperature-sensitive mutations in the putative herpes simplex virus type 1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging and interaction with pUL28 at the nonpermissive temperature. J Virol 82:487-494 (Pubitemid 350309162)
    • (2008) Journal of Virology , vol.82 , Issue.1 , pp. 487-494
    • Yang, K.1    Poon, A.P.W.2    Roizman, B.3    Baines, J.D.4
  • 96
    • 53549123557 scopus 로고    scopus 로고
    • Packaging of a unit length viral genome: The role of nucleotides and the gpD decoration protein in stable nucleocapsid assembly in bacteriophage lambda
    • Yang Q, Maluf NK, Catalano CE (2008b) Packaging of a unit length viral genome: the role of nucleotides and the gpD decoration protein in stable nucleocapsid assembly in bacteriophage lambda. J Mol Biol 383:1037-1048
    • (2008) J Mol Biol , vol.383 , pp. 1037-1048
    • Yang, Q.1    Maluf, N.K.2    Catalano, C.E.3
  • 98
    • 52949145603 scopus 로고    scopus 로고
    • Role of the CCA bulge of prohead RNA of bacteriophage j 29 in DNA packaging
    • Zhao W, Morais MC, Anderson DL, Jardine PJ, Grimes S (2008) Role of the CCA bulge of prohead RNA of bacteriophage j 29 in DNA packaging. J Mol Biol 383:520-528
    • (2008) J Mol Biol , vol.383 , pp. 520-528
    • Zhao, W.1    Morais, M.C.2    Anderson, D.L.3    Jardine, P.J.4    Grimes, S.5
  • 100
    • 38949104355 scopus 로고    scopus 로고
    • A conformational switch in bacteriophage P22 portal protein primes genome injection
    • DOI 10.1016/j.molcel.2007.11.034, PII S1097276508000063
    • Zheng H, Olia AS, Gonen M, Andrews S, Cingolani G, Gonen T (2008) A conformational switch in bacteriophage P22 portal protein primes genome injection. Mol Cell 29:376-383 (Pubitemid 351215935)
    • (2008) Molecular Cell , vol.29 , Issue.3 , pp. 376-383
    • Zheng, H.1    Olia, A.S.2    Gonen, M.3    Andrews, S.4    Cingolani, G.5    Gonen, T.6


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