메뉴 건너뛰기




Volumn 378, Issue 3, 2008, Pages 726-736

Insight into DNA and Protein Transport in Double-Stranded DNA Viruses: The Structure of Bacteriophage N4

Author keywords

bacteriophage N4; cryoelectron microscopy; DNA and protein transport; T = 9 quasi symmetry; virion encapsidated DNA dependent RNA polymerase

Indexed keywords

CAPSID PROTEIN; DNA DIRECTED RNA POLYMERASE; DOUBLE STRANDED DNA; GLYCOPROTEIN 17; GLYCOPROTEIN 50; GLYCOPROTEIN 59; GLYCOPROTEIN 65; GLYCOPROTEIN 66; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 42249109989     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.059     Document Type: Article
Times cited : (83)

References (55)
  • 2
    • 0023688813 scopus 로고
    • Characterization of ion channels involved in the penetration of phage T4 DNA into Escherichia coli cells
    • Boulanger P., and Letellier L. Characterization of ion channels involved in the penetration of phage T4 DNA into Escherichia coli cells. J. Biol. Chem. 263 (1988) 9767-9775
    • (1988) J. Biol. Chem. , vol.263 , pp. 9767-9775
    • Boulanger, P.1    Letellier, L.2
  • 3
    • 0017657414 scopus 로고
    • DNA arrangement in isometric phage heads
    • Earnshaw W.C., and Harrison S.C. DNA arrangement in isometric phage heads. Nature (London) 268 (1977) 598-602
    • (1977) Nature (London) , vol.268 , pp. 598-602
    • Earnshaw, W.C.1    Harrison, S.C.2
  • 4
    • 0018932980 scopus 로고
    • DNA packaging by double-stranded DNA bacteriophages
    • Earnshaw W.C., and Casjens S.R. DNA packaging by double-stranded DNA bacteriophages. Cell 21 (1980) 319-331
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 6
    • 0026726725 scopus 로고
    • Involvement of phage T5 tail proteins and contact sites between the outer and inner membrane of Escherichia coli in phage T5 DNA injection
    • Guihard G., Boulanger P., and Letellier L. Involvement of phage T5 tail proteins and contact sites between the outer and inner membrane of Escherichia coli in phage T5 DNA injection. J. Biol. Chem. 267 (1992) 3173-3178
    • (1992) J. Biol. Chem. , vol.267 , pp. 3173-3178
    • Guihard, G.1    Boulanger, P.2    Letellier, L.3
  • 8
    • 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
  • 9
    • 24944579983 scopus 로고    scopus 로고
    • Changes in bacteriophage T7 virion structure at the initiation of infection
    • Kemp P., Garcia L.R., and Molineux I.J. Changes in bacteriophage T7 virion structure at the initiation of infection. Virology 340 (2005) 307-317
    • (2005) Virology , vol.340 , pp. 307-317
    • Kemp, P.1    Garcia, L.R.2    Molineux, I.J.3
  • 10
    • 34748872268 scopus 로고    scopus 로고
    • Bacteriophage N4
    • Calendar R. (Ed), Oxford University Press, USA
    • Kazmierczak K.M., and Rothman-Denes L.B. Bacteriophage N4. In: Calendar R. (Ed). The Bacteriophages (2006), Oxford University Press, USA 302-314
    • (2006) The Bacteriophages , pp. 302-314
    • Kazmierczak, K.M.1    Rothman-Denes, L.B.2
  • 11
    • 0043102219 scopus 로고
    • Virion-associated RNA polymerase required for bacteriophage N4 development
    • Falco S.C., VanderLaan K., and Rothman-Denes L.B. Virion-associated RNA polymerase required for bacteriophage N4 development. Proc. Natl Acad. Sci. USA 74 (1977) 520-523
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 520-523
    • Falco, S.C.1    VanderLaan, K.2    Rothman-Denes, L.B.3
  • 12
    • 0016148847 scopus 로고
    • Novel transcribing activities in N4-infected Escherichia coli
    • Rothman-Denes L.B., and Schito G.C. Novel transcribing activities in N4-infected Escherichia coli. Virology 60 (1974) 65-72
    • (1974) Virology , vol.60 , pp. 65-72
    • Rothman-Denes, L.B.1    Schito, G.C.2
  • 13
    • 0021099726 scopus 로고
    • Purification and characterization of coliphage N4 RNA polymerase II activity from infected cell extracts
    • Zehring W.A., and Rothman-Denes L.B. Purification and characterization of coliphage N4 RNA polymerase II activity from infected cell extracts. J. Biol. Chem. 258 (1983) 8074-8080
    • (1983) J. Biol. Chem. , vol.258 , pp. 8074-8080
    • Zehring, W.A.1    Rothman-Denes, L.B.2
  • 14
    • 0141595031 scopus 로고    scopus 로고
    • Phage N4 RNA polymerase II recruitment to DNA by a single-stranded DNA binding protein
    • Carter R.C., Demidenko A.A., Hattingh-Willis S., and Rothman-Denes L.B. Phage N4 RNA polymerase II recruitment to DNA by a single-stranded DNA binding protein. Genes Dev. 17 (2003) 2334-2345
    • (2003) Genes Dev. , vol.17 , pp. 2334-2345
    • Carter, R.C.1    Demidenko, A.A.2    Hattingh-Willis, S.3    Rothman-Denes, L.B.4
  • 16
    • 0019190752 scopus 로고
    • DNA-dependent RNA polymerase from bacteriophage N4 virions. Purification and characterization
    • Falco S.C., Zehring W., and Rothman-Denes L.B. DNA-dependent RNA polymerase from bacteriophage N4 virions. Purification and characterization. J. Biol. Chem. 255 (1980) 4339-4347
    • (1980) J. Biol. Chem. , vol.255 , pp. 4339-4347
    • Falco, S.C.1    Zehring, W.2    Rothman-Denes, L.B.3
  • 17
    • 0036846250 scopus 로고    scopus 로고
    • The phage N4 virion RNA polymerase catalytic domain is related to single-subunit RNA polymerases
    • Kazmierczak K.M., Davydova E.K., Mustaev A.A., and Rothman-Denes L.B. The phage N4 virion RNA polymerase catalytic domain is related to single-subunit RNA polymerases. EMBO J. 21 (2002) 5815-5823
    • (2002) EMBO J. , vol.21 , pp. 5815-5823
    • Kazmierczak, K.M.1    Davydova, E.K.2    Mustaev, A.A.3    Rothman-Denes, L.B.4
  • 19
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., and Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature (London) 439 (2006) 612-616
    • (2006) Nature (London) , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 20
    • 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
  • 21
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of φ{symbol}29
    • Morais M.C., Choi K.H., Koti J.S., Chipman P.R., Anderson D.L., and Rossmann M.G. Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of φ{symbol}29. Mol. Cell 18 (2005) 149-159
    • (2005) Mol. Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 23
    • 18844400837 scopus 로고    scopus 로고
    • Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
    • Fokine A., Leiman P.G., Shneider M.M., Ahvazi B., Boeshans K.M., Steven A.C., et al. 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
    • (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
  • 25
    • 0035878724 scopus 로고    scopus 로고
    • Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements
    • Schaffer A.A., Aravind L., Madden T.L., Shavirin S., Spouge J.L., Wolf Y.I., et al. Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements. Nucleic Acids Res. 29 (2001) 2994-3005
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2994-3005
    • Schaffer, A.A.1    Aravind, L.2    Madden, T.L.3    Shavirin, S.4    Spouge, J.L.5    Wolf, Y.I.6
  • 27
    • 0036893072 scopus 로고    scopus 로고
    • Rapid protein domain assignment from amino acid sequence using predicted secondary structure
    • Marsden R.L., McGuffin L.J., and Jones D.T. Rapid protein domain assignment from amino acid sequence using predicted secondary structure. Protein Sci. 11 (2002) 2814-2824
    • (2002) Protein Sci. , vol.11 , pp. 2814-2824
    • Marsden, R.L.1    McGuffin, L.J.2    Jones, D.T.3
  • 28
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292 (1999) 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.1
  • 29
    • 0027085892 scopus 로고
    • Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, cooperativity, and super-stabilization by soc binding
    • Steven A.C., Greenstone H.L., Booy F.P., Black L.W., and Ross P.D. Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, cooperativity, and super-stabilization by soc binding. J. Mol. Biol. 228 (1992) 870-884
    • (1992) J. Mol. Biol. , vol.228 , pp. 870-884
    • Steven, A.C.1    Greenstone, H.L.2    Booy, F.P.3    Black, L.W.4    Ross, P.D.5
  • 30
    • 14644422590 scopus 로고    scopus 로고
    • Nucleotide sequence of the head assembly gene cluster of bacteriophage L and decoration protein characterization
    • Gilcrease E.B., Winn-Stapley D.A., Hewitt F.C., Joss L., and Casjens S.R. Nucleotide sequence of the head assembly gene cluster of bacteriophage L and decoration protein characterization. J. Bacteriol. 187 (2005) 2050-2057
    • (2005) J. Bacteriol. , vol.187 , pp. 2050-2057
    • Gilcrease, E.B.1    Winn-Stapley, D.A.2    Hewitt, F.C.3    Joss, L.4    Casjens, S.R.5
  • 31
    • 0019304084 scopus 로고
    • Outer surface protein of bacteriophage lambda
    • Imber R., Tsugita A., Wurtz M., and Hohn T. Outer surface protein of bacteriophage lambda. J. Mol. Biol. 139 (1980) 277-295
    • (1980) J. Mol. Biol. , vol.139 , pp. 277-295
    • Imber, R.1    Tsugita, A.2    Wurtz, M.3    Hohn, T.4
  • 32
    • 33646191863 scopus 로고    scopus 로고
    • Ig-like domains on bacteriophage: a tale of promiscuity and deceit
    • Fraser J.S., Yu Z., Maxwell K.L., and Davidson A.R. Ig-like domains on bacteriophage: a tale of promiscuity and deceit. J. Mol. Biol. 359 (2006) 496-507
    • (2006) J. Mol. Biol. , vol.359 , pp. 496-507
    • Fraser, J.S.1    Yu, Z.2    Maxwell, K.L.3    Davidson, A.R.4
  • 33
    • 33646353426 scopus 로고    scopus 로고
    • Highly discriminatory binding of capsid-cementing proteins in bacteriophage L
    • Tang L., Gilcrease E.B., Casjens S.R., and Johnson J.E. Highly discriminatory binding of capsid-cementing proteins in bacteriophage L. Structure 14 (2006) 837-845
    • (2006) Structure , vol.14 , pp. 837-845
    • Tang, L.1    Gilcrease, E.B.2    Casjens, S.R.3    Johnson, J.E.4
  • 34
    • 0035909970 scopus 로고    scopus 로고
    • Cryoelectron microscopy of λ phage DNA condensates in vitreous ice: the fine structure of DNA toroids
    • Hud N.V., and Downing K.H. Cryoelectron microscopy of λ phage DNA condensates in vitreous ice: the fine structure of DNA toroids. Proc. Natl Acad. Sci. USA 98 (2001) 14925-14930
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14925-14930
    • Hud, N.V.1    Downing, K.H.2
  • 35
    • 0035783057 scopus 로고    scopus 로고
    • Cryoelectron-microscopy image reconstruction of symmetry mismatches in bacteriophage φ{symbol}29
    • Morais M.C., Tao Y., Olson N.H., Grimes S., Jardine P.J., Anderson D.L., et al. Cryoelectron-microscopy image reconstruction of symmetry mismatches in bacteriophage φ{symbol}29. J. Struct. Biol. 135 (2001) 38-46
    • (2001) J. Struct. Biol. , vol.135 , pp. 38-46
    • Morais, M.C.1    Tao, Y.2    Olson, N.H.3    Grimes, S.4    Jardine, P.J.5    Anderson, D.L.6
  • 37
    • 33646785677 scopus 로고    scopus 로고
    • Fold recognition and accurate sequence-structure alignment of sequences directing β-sheet proteins
    • McDonnell A.V., Menke M., Palmer N., King J., Cowen L., and Berger B. Fold recognition and accurate sequence-structure alignment of sequences directing β-sheet proteins. Proteins 63 (2006) 976-985
    • (2006) Proteins , vol.63 , pp. 976-985
    • McDonnell, A.V.1    Menke, M.2    Palmer, N.3    King, J.4    Cowen, L.5    Berger, B.6
  • 38
    • 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
  • 40
    • 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
  • 42
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage P2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli S., Desmyter A., Verrips C.T., de Haard H.J.W., Moineau S., and Cambillau C. Lactococcal bacteriophage P2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13 (2005) 85-89
    • (2005) Nat. Struct. Mol. Biol. , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    de Haard, H.J.W.4    Moineau, S.5    Cambillau, C.6
  • 43
    • 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
  • 44
    • 33745506037 scopus 로고    scopus 로고
    • The structure of an infectious P22 virion shows the signal for headful DNA packaging
    • Lander G.C., Tang L., Casjens S.R., Gilcrease E.B., Prevelige P., Poliakov A., et al. The structure of an infectious P22 virion shows the signal for headful DNA packaging. Science 312 (2006) 1791-1795
    • (2006) Science , vol.312 , pp. 1791-1795
    • Lander, G.C.1    Tang, L.2    Casjens, S.R.3    Gilcrease, E.B.4    Prevelige, P.5    Poliakov, A.6
  • 45
    • 0015526899 scopus 로고
    • Bacteriophage T7
    • Studier F.W. Bacteriophage T7. Science 176 (1972) 367-376
    • (1972) Science , vol.176 , pp. 367-376
    • Studier, F.W.1
  • 47
    • 15244343074 scopus 로고    scopus 로고
    • Structure of the connector of bacteriophage T7 at 8 Å resolution: structural homologies of a basic component of a DNA translocating machinery
    • Agirrezabala X., Martín-Benito J., Valle M., González J.M., Valencia A., Valpuesta J.M., and Carrascosa J.L. Structure of the connector of bacteriophage T7 at 8 Å resolution: structural homologies of a basic component of a DNA translocating machinery. J. Mol. Biol. 347 (2005) 895-902
    • (2005) J. Mol. Biol. , vol.347 , pp. 895-902
    • Agirrezabala, X.1    Martín-Benito, J.2    Valle, M.3    González, J.M.4    Valencia, A.5    Valpuesta, J.M.6    Carrascosa, J.L.7
  • 49
  • 50
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy
    • Orlova E.V., Gowen B., Dröge A., Stiege A., Weise F., Lurz R., et al. Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy. EMBO J. 22 (2003) 1255-1262
    • (2003) EMBO J. , vol.22 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Dröge, A.3    Stiege, A.4    Weise, F.5    Lurz, R.6
  • 51
    • 0024308487 scopus 로고
    • Genetic analysis of bacteriophage N4 adsorption
    • Kiino D.R., and Rothman-Denes L.B. Genetic analysis of bacteriophage N4 adsorption. J. Bacteriol. 171 (1989) 4595-4602
    • (1989) J. Bacteriol. , vol.171 , pp. 4595-4602
    • Kiino, D.R.1    Rothman-Denes, L.B.2
  • 52
    • 0032515102 scopus 로고    scopus 로고
    • Activity of foreign proteins targeted within the bacteriophage T4 head and prohead: implications for packaged DNA structure
    • Mullaney J.M., and Black L.W. Activity of foreign proteins targeted within the bacteriophage T4 head and prohead: implications for packaged DNA structure. J. Mol. Biol. 283 (1998) 913-929
    • (1998) J. Mol. Biol. , vol.283 , pp. 913-929
    • Mullaney, J.M.1    Black, L.W.2
  • 53
    • 0036724258 scopus 로고    scopus 로고
    • N4 RNA polymerase II, a heterodimeric RNA polymerase with homology to the single-subunit family of RNA polymerases
    • Willis S.H., Kazmierczak K.M., Carter R.H., and Rothman-Denes L.B. N4 RNA polymerase II, a heterodimeric RNA polymerase with homology to the single-subunit family of RNA polymerases. J. Bacteriol. 184 (2002) 4952-4961
    • (2002) J. Bacteriol. , vol.184 , pp. 4952-4961
    • Willis, S.H.1    Kazmierczak, K.M.2    Carter, R.H.3    Rothman-Denes, L.B.4
  • 54
    • 42249084293 scopus 로고    scopus 로고
    • Willis, S. H. (1997). Analysis of Bacteriophage N4 RNAPII. PhD thesis, The University of Chicago, Chicago, IL.
    • Willis, S. H. (1997). Analysis of Bacteriophage N4 RNAPII. PhD thesis, The University of Chicago, Chicago, IL.
  • 55
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.