메뉴 건너뛰기




Volumn 18, Issue 6, 2010, Pages 700-709

Evolution in Action: N and C Termini of Subunits in Related T = 4 Viruses Exchange Roles as Molecular Switches

Author keywords

Evo_Ecol; Microbio; Proteins

Indexed keywords

CAPSID PROTEIN; RNA BINDING PROTEIN;

EID: 77953579261     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.03.010     Document Type: Article
Times cited : (17)

References (51)
  • 3
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker M.L., Jiang W., Rixon F.J., Chiu W. Common ancestry of herpesviruses and tailed DNA bacteriophages. J. Virol. 2005, 79:14967-14970.
    • (2005) J. Virol. , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 5
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • Bothner B., Dong X.F., Bibbs L., Johnson J.E., Siuzdak G. Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry. J. Biol. Chem. 1998, 273:673-676.
    • (1998) J. Biol. Chem. , vol.273 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 6
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger A.T. Version 1.2 of the crystallography and NMR system. Nat. Protoc. 2007, 2:2728-2733.
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 9
    • 0028773272 scopus 로고
    • Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography
    • Cheng R.H., Reddy V.S., Olson N.H., Fisher A.J., Baker T.S., Johnson J.E. Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography. Structure 1994, 2:271-282.
    • (1994) Structure , vol.2 , pp. 271-282
    • Cheng, R.H.1    Reddy, V.S.2    Olson, N.H.3    Fisher, A.J.4    Baker, T.S.5    Johnson, J.E.6
  • 11
    • 33746414364 scopus 로고    scopus 로고
    • Considerations for the refinement of low-resolution crystal structures
    • DeLaBarre B., Brunger A.T. Considerations for the refinement of low-resolution crystal structures. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:923-932.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 923-932
    • DeLaBarre, B.1    Brunger, A.T.2
  • 12
    • 33847042739 scopus 로고    scopus 로고
    • Protein-RNA interactions: structural analysis and functional classes
    • Ellis J.J., Broom M., Jones S. Protein-RNA interactions: structural analysis and functional classes. Proteins 2007, 66:903-911.
    • (2007) Proteins , vol.66 , pp. 903-911
    • Ellis, J.J.1    Broom, M.2    Jones, S.3
  • 13
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • Fisher A.J., Johnson J.E. Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 1993, 361:176-179.
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 15
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 16
    • 0026660237 scopus 로고
    • The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties
    • Ghisolfi L., Joseph G., Amalric F., Erard M. The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties. J. Biol. Chem. 1992, 267:2955-2959.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2955-2959
    • Ghisolfi, L.1    Joseph, G.2    Amalric, F.3    Erard, M.4
  • 18
    • 1242319463 scopus 로고    scopus 로고
    • The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation
    • Helgstrand C., Munshi S., Johnson J.E., Liljas L. The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation. Virology 2004, 318:192-203.
    • (2004) Virology , vol.318 , pp. 192-203
    • Helgstrand, C.1    Munshi, S.2    Johnson, J.E.3    Liljas, L.4
  • 20
    • 0001146459 scopus 로고    scopus 로고
    • Packaging and release of the viral genome
    • Oxford University Press, New York, R.M. Burnett, W. Chiu, R. Garcea (Eds.)
    • Johnson J.E., Rueckert R.R. Packaging and release of the viral genome. Structural Biology of Viruses 1997, 269-287. Oxford University Press, New York. R.M. Burnett, W. Chiu, R. Garcea (Eds.).
    • (1997) Structural Biology of Viruses , pp. 269-287
    • Johnson, J.E.1    Rueckert, R.R.2
  • 21
    • 0031588020 scopus 로고    scopus 로고
    • Quasi-equivalent viruses: a paradigm for protein assemblies
    • Johnson J.E., Speir J.A. Quasi-equivalent viruses: a paradigm for protein assemblies. J. Mol. Biol. 1997, 269:665-675.
    • (1997) J. Mol. Biol. , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 24
    • 30044450170 scopus 로고    scopus 로고
    • Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses
    • Khayat R., Tang L., Larson E.T., Lawrence C.M., Young M., Johnson J.E. Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc. Natl. Acad. Sci. USA 2005, 102:18944-18949.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18944-18949
    • Khayat, R.1    Tang, L.2    Larson, E.T.3    Lawrence, C.M.4    Young, M.5    Johnson, J.E.6
  • 26
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 28
    • 58149517675 scopus 로고    scopus 로고
    • Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid
    • Matsui T., Lander G., Johnson J.E. Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid. J. Virol. 2009, 83:1126-1134.
    • (2009) J. Virol. , vol.83 , pp. 1126-1134
    • Matsui, T.1    Lander, G.2    Johnson, J.E.3
  • 29
    • 33750997616 scopus 로고    scopus 로고
    • Protein-RNA interactions: exploring binding patterns with a three-dimensional superposition analysis of high resolution structures
    • Morozova N., Allers J., Myers J., Shamoo Y. Protein-RNA interactions: exploring binding patterns with a three-dimensional superposition analysis of high resolution structures. Bioinformatics 2006, 22:2746-2752.
    • (2006) Bioinformatics , vol.22 , pp. 2746-2752
    • Morozova, N.1    Allers, J.2    Myers, J.3    Shamoo, Y.4
  • 30
    • 0030576341 scopus 로고    scopus 로고
    • The 2.8 Å structure of a T = 4 animal virus and its implications for membrane translocation of RNA
    • Munshi S., Liljas L., Cavarelli J., Bomu W., McKinney B., Reddy V., Johnson J.E. The 2.8 Å structure of a T = 4 animal virus and its implications for membrane translocation of RNA. J. Mol. Biol. 1996, 261:1-10.
    • (1996) J. Mol. Biol. , vol.261 , pp. 1-10
    • Munshi, S.1    Liljas, L.2    Cavarelli, J.3    Bomu, W.4    McKinney, B.5    Reddy, V.6    Johnson, J.E.7
  • 31
    • 0025569309 scopus 로고
    • The three-dimensional structure of frozen-hydrated Nudaurelia capensis beta virus, a T = 4 insect virus
    • Olson N.H., Baker T.S., Johnson J.E., Hendry D.A. The three-dimensional structure of frozen-hydrated Nudaurelia capensis beta virus, a T = 4 insect virus. J. Struct. Biol. 1990, 105:111-122.
    • (1990) J. Struct. Biol. , vol.105 , pp. 111-122
    • Olson, N.H.1    Baker, T.S.2    Johnson, J.E.3    Hendry, D.A.4
  • 33
    • 0037440765 scopus 로고    scopus 로고
    • Providence virus: a new member of the Tetraviridae that infects cultured insect cells
    • Pringle F.M., Johnson K.N., Goodman C.L., McIntosh A.H., Ball L.A. Providence virus: a new member of the Tetraviridae that infects cultured insect cells. Virology 2003, 306:359-370.
    • (2003) Virology , vol.306 , pp. 359-370
    • Pringle, F.M.1    Johnson, K.N.2    Goodman, C.L.3    McIntosh, A.H.4    Ball, L.A.5
  • 34
    • 0031658922 scopus 로고    scopus 로고
    • Specific encapsidation of nodavirus RNAs is mediated through the C terminus of capsid precursor protein alpha
    • Schneemann A., Marshall D. Specific encapsidation of nodavirus RNAs is mediated through the C terminus of capsid precursor protein alpha. J. Virol. 1998, 72:8738-8746.
    • (1998) J. Virol. , vol.72 , pp. 8738-8746
    • Schneemann, A.1    Marshall, D.2
  • 35
    • 0031606858 scopus 로고    scopus 로고
    • The structure and function of nodavirus particles: a paradigm for understanding chemical biology
    • Schneemann A., Reddy V., Johnson J.E. The structure and function of nodavirus particles: a paradigm for understanding chemical biology. Adv. Virus Res. 1998, 50:381-446.
    • (1998) Adv. Virus Res. , vol.50 , pp. 381-446
    • Schneemann, A.1    Reddy, V.2    Johnson, J.E.3
  • 40
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow R.W., Guerra C.A., Noor A.M., Myint H.Y., Hay S.I. The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 2005, 434:214-217.
    • (2005) Nature , vol.434 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 41
    • 77950682411 scopus 로고    scopus 로고
    • Tetraviruses
    • Elsevier, Oxford, B.W.J. Mahy, M.H.V. van Regenmortel (Eds.)
    • Speir J.A., Johnson J.E. Tetraviruses. Encyclopedia of Virology 2008, 27-37. Elsevier, Oxford. B.W.J. Mahy, M.H.V. van Regenmortel (Eds.).
    • (2008) Encyclopedia of Virology , pp. 27-37
    • Speir, J.A.1    Johnson, J.E.2
  • 42
    • 79960420311 scopus 로고    scopus 로고
    • Virus Particle Structure: Nonenveloped Viruses
    • Elsevier, Oxford, B.W.J. Mahy, M.H.V. van Regenmortel (Eds.)
    • Speir J.A., Johnson J.E. Virus Particle Structure: Nonenveloped Viruses. Encyclopedia of Virology 2008, 380-393. Elsevier, Oxford. B.W.J. Mahy, M.H.V. van Regenmortel (Eds.).
    • (2008) Encyclopedia of Virology , pp. 380-393
    • Speir, J.A.1    Johnson, J.E.2
  • 43
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy
    • Speir J.A., Munshi S., Wang G., Baker T.S., Johnson J.E. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure 1995, 3:63-78.
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 46
    • 13244259151 scopus 로고    scopus 로고
    • Folding and particle assembly are disrupted by single point mutations near the autocatalytic site of Nudaurelia capensis ω virus capsid protein
    • Taylor D.J., Johnson J.E. Folding and particle assembly are disrupted by single point mutations near the autocatalytic site of Nudaurelia capensis ω virus capsid protein. Protein Sci. 2005, 14:401-408.
    • (2005) Protein Sci. , vol.14 , pp. 401-408
    • Taylor, D.J.1    Johnson, J.E.2
  • 47
    • 29144442284 scopus 로고    scopus 로고
    • Preliminary x-ray characterization of authentic Providence virus and attempts to express its coat protein gene in recombinant baculovirus
    • Taylor D.J., Speir J.A., Reddy V., Cingolani G., Pringle F.M., Ball L.A., Johnson J.E. Preliminary x-ray characterization of authentic Providence virus and attempts to express its coat protein gene in recombinant baculovirus. Arch. Virol. 2006, 151:155-165.
    • (2006) Arch. Virol. , vol.151 , pp. 155-165
    • Taylor, D.J.1    Speir, J.A.2    Reddy, V.3    Cingolani, G.4    Pringle, F.M.5    Ball, L.A.6    Johnson, J.E.7
  • 48
    • 1542347791 scopus 로고    scopus 로고
    • Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length
    • Tihova M., Dryden K.A., Le T.V., Harvey S.C., Johnson J.E., Yeager M., Schneemann A. Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length. J. Virol. 2004, 78:2897-2905.
    • (2004) J. Virol. , vol.78 , pp. 2897-2905
    • Tihova, M.1    Dryden, K.A.2    Le, T.V.3    Harvey, S.C.4    Johnson, J.E.5    Yeager, M.6    Schneemann, A.7
  • 49
    • 51349094158 scopus 로고    scopus 로고
    • Recent insights into the biology and biomedical applications of Flock House virus
    • Venter P.A., Schneemann A. Recent insights into the biology and biomedical applications of Flock House virus. Cell. Mol. Life Sci. 2008, 65:2675-2687.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2675-2687
    • Venter, P.A.1    Schneemann, A.2
  • 50
    • 42749096469 scopus 로고    scopus 로고
    • Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2
    • Zhang X., Perugini M.A., Yao S., Adda C.G., Murphy V.J., Low A., Anders R.F., Norton R.S. Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. J. Mol. Biol. 2008, 379:105-121.
    • (2008) J. Mol. Biol. , vol.379 , pp. 105-121
    • Zhang, X.1    Perugini, M.A.2    Yao, S.3    Adda, C.G.4    Murphy, V.J.5    Low, A.6    Anders, R.F.7    Norton, R.S.8
  • 51
    • 0028321381 scopus 로고
    • Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue
    • Zlotnick A., Reddy V.S., Dasgupta R., Schneemann A., Ray W.J., Rueckert R.R., Johnson J.E. Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue. J. Biol. Chem. 1994, 269:13680-13684.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13680-13684
    • Zlotnick, A.1    Reddy, V.S.2    Dasgupta, R.3    Schneemann, A.4    Ray, W.J.5    Rueckert, R.R.6    Johnson, J.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.