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Volumn 17, Issue 2, 2007, Pages 237-243

DNA packaging and delivery machines in tailed bacteriophages

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; PROTEIN P22;

EID: 34147123766     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.03.011     Document Type: Review
Times cited : (106)

References (36)
  • 1
    • 17044440108 scopus 로고    scopus 로고
    • Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    • Steven A.C., Heymann J.B., Cheng N., Trus B.L., and Conway J.F. Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity. Curr Opin Struct Biol 15 (2005) 227-236
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 227-236
    • Steven, A.C.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Conway, J.F.5
  • 2
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher S., Miller S., Baxa U., Budisa N., Weintraub A., Seckler R., and Huber R. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage. J Mol Biol 267 (1997) 865-880
    • (1997) J Mol Biol , vol.267 , pp. 865-880
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 3
    • 0029764093 scopus 로고    scopus 로고
    • Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors
    • Steinbacher S., Baxa U., Miller S., Weintraub A., Seckler R., and Huber R. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc Natl Acad Sci USA 93 (1996) 10584-10588
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10584-10588
    • Steinbacher, S.1    Baxa, U.2    Miller, S.3    Weintraub, A.4    Seckler, R.5    Huber, R.6
  • 4
    • 0034703226 scopus 로고    scopus 로고
    • Topologically linked protein rings in the bacteriophage HK97 capsid
    • Wikoff W.R., Liljas L., Duda R., Tsuruta H., Hendrix R., and Johnson J. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289 (2000) 2129-2133
    • (2000) Science , vol.289 , pp. 2129-2133
    • Wikoff, W.R.1    Liljas, L.2    Duda, R.3    Tsuruta, H.4    Hendrix, R.5    Johnson, J.6
  • 5
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang W., Li Z., Zhang Z., Baker M.L., Prevelige Jr. P.E., and Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol 10 (2003) 131-135
    • (2003) Nat Struct Biol , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 6
    • 18844400837 scopus 로고    scopus 로고
    • Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
    • The first atomic structure to confirm the similarity of the folds of HK97 and another bacteriophage.
    • Fokine A., Leiman P.G., Shneider M.M., Ahvazi B., Boeshans K.M., Steven A.C., Black L.W., Mesyanzhinov V.V., and Rossmann M.G. Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc Natl Acad Sci USA 102 (2005) 7163-7168. The first atomic structure to confirm the similarity of the folds of HK97 and another bacteriophage.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7163-7168
    • Fokine, A.1    Leiman, P.G.2    Shneider, M.M.3    Ahvazi, B.4    Boeshans, K.M.5    Steven, A.C.6    Black, L.W.7    Mesyanzhinov, V.V.8    Rossmann, M.G.9
  • 7
    • 0035864288 scopus 로고    scopus 로고
    • The structure of isometric capsids of bacteriophage T4
    • Olson N.H., Gingery M., Eiserling F.A., and Baker T.S. The structure of isometric capsids of bacteriophage T4. Virology 279 (2001) 385-391
    • (2001) Virology , vol.279 , pp. 385-391
    • Olson, N.H.1    Gingery, M.2    Eiserling, F.A.3    Baker, T.S.4
  • 8
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • EM evidence that the shell-forming portion of the herpesvirus subunit shares structural similarity with HK97.
    • Baker M.L., Jiang W., Rixon F.J., and Chiu W. Common ancestry of herpesviruses and tailed DNA bacteriophages. J Virol 79 (2005) 14967-14970. EM evidence that the shell-forming portion of the herpesvirus subunit shares structural similarity with HK97.
    • (2005) J Virol , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 9
    • 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., and Baker T.S. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95 (1998) 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
  • 11
    • 33750450852 scopus 로고    scopus 로고
    • Structural changes of bacteriophage phi29 upon DNA packaging and release
    • This paper describes the asymmetric reconstruction of a phage with an elongated capsid. The X-ray model of the φ{symbol}29 portal was placed in the cryo-EM density, providing the only example of a positioned and oriented portal atomic model in a capsid.
    • Xiang Y., Morais M.C., Battisti A.J., Grimes S., Jardine P.J., Anderson D.L., and Rossmann M.G. Structural changes of bacteriophage phi29 upon DNA packaging and release. EMBO J 25 (2006) 5229-5239. This paper describes the asymmetric reconstruction of a phage with an elongated capsid. The X-ray model of the φ{symbol}29 portal was placed in the cryo-EM density, providing the only example of a positioned and oriented portal atomic model in a capsid.
    • (2006) EMBO J , vol.25 , pp. 5229-5239
    • Xiang, Y.1    Morais, M.C.2    Battisti, A.J.3    Grimes, S.4    Jardine, P.J.5    Anderson, D.L.6    Rossmann, M.G.7
  • 14
    • 13444283414 scopus 로고    scopus 로고
    • Control of bacteriophage T4 tail lysozyme activity during the infection process
    • Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., and Arisaka F. Control of bacteriophage T4 tail lysozyme activity during the infection process. J Mol Biol 346 (2005) 1013-1020
    • (2005) J Mol Biol , vol.346 , pp. 1013-1020
    • Kanamaru, S.1    Ishiwata, Y.2    Suzuki, T.3    Rossmann, M.G.4    Arisaka, F.5
  • 16
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., and Rossmann M.G. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 118 (2004) 419-429
    • (2004) Cell , vol.118 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 18
    • 0042827209 scopus 로고    scopus 로고
    • Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment
    • Cerritelli M.E., Conway J.F., Cheng N., Trus B.L., and Steven A.C. Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment. Adv Protein Chem 64 (2003) 301-323
    • (2003) Adv Protein Chem , vol.64 , pp. 301-323
    • Cerritelli, M.E.1    Conway, J.F.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 19
    • 0037436386 scopus 로고    scopus 로고
    • A second symmetry mismatch at the portal vertex of bacteriophage T7: 8-fold symmetry in the procapsid core
    • Cerritelli M.E., Trus B.L., Smith C.S., Cheng N., Conway J.F., and Steven A.C. A second symmetry mismatch at the portal vertex of bacteriophage T7: 8-fold symmetry in the procapsid core. J Mol Biol 327 (2003) 1-6
    • (2003) J Mol Biol , vol.327 , pp. 1-6
    • Cerritelli, M.E.1    Trus, B.L.2    Smith, C.S.3    Cheng, N.4    Conway, J.F.5    Steven, A.C.6
  • 20
    • 27744572947 scopus 로고    scopus 로고
    • Maturation of phage T7 involves structural modification of both shell and inner core components
    • Moderate-resolution asymmetric reconstructions of the T7 procapsid and mature particle. The only example to date of an asymmetric reconstruction of a procapsid.
    • Agirrezabala X., Martin-Benito J., Caston J.R., Miranda R., Valpuesta J.M., and Carrascosa J.L. Maturation of phage T7 involves structural modification of both shell and inner core components. EMBO J 24 (2005) 3820-3829. Moderate-resolution asymmetric reconstructions of the T7 procapsid and mature particle. The only example to date of an asymmetric reconstruction of a procapsid.
    • (2005) EMBO J , vol.24 , pp. 3820-3829
    • Agirrezabala, X.1    Martin-Benito, J.2    Caston, J.R.3    Miranda, R.4    Valpuesta, J.M.5    Carrascosa, J.L.6
  • 21
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • A reconstruction showing exceptional detail for the portal, core and associated DNA. This phage, in common with φ{symbol}29, has flexible tailspikes, but the tailspikes have very similar structures at each of the six positions relative to the capsid.
    • Jiang W., Chang J., Jakana J., Weigele P., King J., and Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 439 (2006) 612-616. A reconstruction showing exceptional detail for the portal, core and associated DNA. This phage, in common with φ{symbol}29, has flexible tailspikes, but the tailspikes have very similar structures at each of the six positions relative to the capsid.
    • (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
  • 22
    • 33745506037 scopus 로고    scopus 로고
    • The structure of an infectious P22 virion shows the signal for headful DNA packaging
    • An asymmetric structure with a portal in the capsid that could be compared with the ectopically expressed and assembled portal is described. The marked difference in structure suggested that the portal may change conformation under the high pressure of the packaged DNA, signaling that the particle is full. The atomic model of the tailspike trimeric proteins fits the EM density with exceptional precision.
    • Lander G.C., Tang L., Casjens S.R., Gilcrease E.B., Prevelige P., Poliakov A., Potter C.S., Carragher B., and Johnson J.E. The structure of an infectious P22 virion shows the signal for headful DNA packaging. Science 312 (2006) 1791-1795. An asymmetric structure with a portal in the capsid that could be compared with the ectopically expressed and assembled portal is described. The marked difference in structure suggested that the portal may change conformation under the high pressure of the packaged DNA, signaling that the particle is full. The atomic model of the tailspike trimeric proteins fits the EM density with exceptional precision.
    • (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    Potter, C.S.7    Carragher, B.8    Johnson, J.E.9
  • 23
    • 33744811672 scopus 로고    scopus 로고
    • Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery
    • ••], revealing closely similar portal conformations, DNA packaging and tailspike conformations.
    • ••], revealing closely similar portal conformations, DNA packaging and tailspike conformations.
    • (2006) Structure , vol.14 , pp. 1073-1082
    • Chang, J.1    Weigele, P.2    King, J.3    Chiu, W.4    Jiang, W.5
  • 24
    • 21844456877 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacteriophage P22 tail machine
    • The moderate-resolution structure of the tail machine of P22 and the isolated portal is described in this research. The difference in conformation between the portal in this structure and that in the particle suggests that it changes conformation under pressure from DNA packaging.
    • Tang L., Marion W.R., Cingolani G., Prevelige P.E., and Johnson J.E. Three-dimensional structure of the bacteriophage P22 tail machine. EMBO J 24 (2005) 2087-2095. The moderate-resolution structure of the tail machine of P22 and the isolated portal is described in this research. The difference in conformation between the portal in this structure and that in the particle suggests that it changes conformation under pressure from DNA packaging.
    • (2005) EMBO J , vol.24 , pp. 2087-2095
    • Tang, L.1    Marion, W.R.2    Cingolani, G.3    Prevelige, P.E.4    Johnson, J.E.5
  • 25
    • 0026538238 scopus 로고
    • Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA
    • Casjens S., Wyckoff E., Hayden M., Sampson L., Eppler K., Randall S., Moreno E.T., and Serwer P. Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA. J Mol Biol 224 (1992) 1055-1074
    • (1992) J Mol Biol , vol.224 , pp. 1055-1074
    • Casjens, S.1    Wyckoff, E.2    Hayden, M.3    Sampson, L.4    Eppler, K.5    Randall, S.6    Moreno, E.T.7    Serwer, P.8
  • 26
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage straight 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., and Bustamante C. The bacteriophage straight 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
  • 27
    • 0034646575 scopus 로고    scopus 로고
    • Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus
    • Sun Y., Parker M.H., Weigele P., Casjens S., Prevelige Jr. P.E., and Krishna N.R. Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus. J Mol Biol 297 (2000) 1195-1202
    • (2000) J Mol Biol , vol.297 , pp. 1195-1202
    • Sun, Y.1    Parker, M.H.2    Weigele, P.3    Casjens, S.4    Prevelige Jr., P.E.5    Krishna, N.R.6
  • 28
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain
    • Tao Y., Strelkov S.V., Mesyanzhinov V.V., and Rossmann M.G. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5 (1997) 789-798
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 33
    • 33646029067 scopus 로고    scopus 로고
    • Evolution of bacteriophage tails: Structure of T4 gene product 10
    • Leiman P.G., Shneider M.M., Mesyanzhinov V.V., and Rossmann M.G. Evolution of bacteriophage tails: Structure of T4 gene product 10. J Mol Biol 358 (2006) 912-921
    • (2006) J Mol Biol , vol.358 , pp. 912-921
    • Leiman, P.G.1    Shneider, M.M.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 36
    • 33947213307 scopus 로고    scopus 로고
    • Experimental test of connector rotation during DNA packaging into bacteriophage Phi29 capsids
    • This paper describes experiments that virtually guarantee that there is no rotation of the portal (connector) assembly during DNA packaging, thus resolving a controversy that has gone on for nearly 25 years.
    • Hugel T., Michaelis J., Hetherington C.L., Jardine P.J., Grimes S., Walter J.M., Falk W., Anderson D.L., and Bustamante C. Experimental test of connector rotation during DNA packaging into bacteriophage Phi29 capsids. PLoS Biol 5 (2007) e59. This paper describes experiments that virtually guarantee that there is no rotation of the portal (connector) assembly during DNA packaging, thus resolving a controversy that has gone on for nearly 25 years.
    • (2007) PLoS Biol , vol.5
    • Hugel, T.1    Michaelis, J.2    Hetherington, C.L.3    Jardine, P.J.4    Grimes, S.5    Walter, J.M.6    Falk, W.7    Anderson, D.L.8    Bustamante, C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.