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Volumn 292, Issue 1, 1999, Pages 65-73

Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein

Author keywords

Cryo electron microscopy; Icosahedral 3D reconstruction; Ty retrotransposon; Virus like particles

Indexed keywords

CAPSID PROTEIN;

EID: 0033543555     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3055     Document Type: Article
Times cited : (27)

References (45)
  • 1
    • 0023649679 scopus 로고
    • The functions and relationships of Ty1-VLP proteins in yeast reflect those of mammalian retroviral proteins
    • Adams S. E., Mellor J., Gull K., Sim R. B., Tuite M. F., Kingsman S. M., Kingsman A. J. The functions and relationships of Ty1-VLP proteins in yeast reflect those of mammalian retroviral proteins. Cell. 49:1987;111-119.
    • (1987) Cell , vol.49 , pp. 111-119
    • Adams, S.E.1    Mellor, J.2    Gull, K.3    Sim, R.B.4    Tuite, M.F.5    Kingsman, S.M.6    Kingsman, A.J.7
  • 2
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T. S., Cheng R. H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:1996;120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 3
    • 0000368742 scopus 로고
    • Yeast transposable elements
    • J. R. Broach, J. R. Pringle, & E. W. Jones. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Boeke J. D., Sandmeyer S. B. Yeast transposable elements. Broach J. R., Pringle J. R., Jones E. W. Molecular and Cellular Biology of the yeast Saccharomyces cerevisiae. 1991;193-261 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1991) Molecular and Cellular Biology of the Yeast Saccharomyces Cerevisiae , pp. 193-261
    • Boeke, J.D.1    Sandmeyer, S.B.2
  • 4
    • 0023990722 scopus 로고
    • The Saccharomyces cerevisiae genome contains functional and bon-functional copies of transposon Ty1
    • Boeke J. D., Eichinger D., Castrillon D., Fink G. R. The Saccharomyces cerevisiae genome contains functional and bon-functional copies of transposon Ty1. Mol. Cell. Biol. 8:1988;1432-1442.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1432-1442
    • Boeke, J.D.1    Eichinger, D.2    Castrillon, D.3    Fink, G.R.4
  • 5
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S. A., Crowther R. A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 6
    • 0028789680 scopus 로고
    • Analysis of TYA protein regions necessary for formation of the Ty1 virus-like particle structure
    • Brookman J. L., Stott A. J., Cheeseman P. J., Adamson C. S., Holmes D., Cole J., Burns N. R. Analysis of TYA protein regions necessary for formation of the Ty1 virus-like particle structure. Virology. 212:1995a;69-76.
    • (1995) Virology , vol.212 , pp. 69-76
    • Brookman, J.L.1    Stott, A.J.2    Cheeseman, P.J.3    Adamson, C.S.4    Holmes, D.5    Cole, J.6    Burns, N.R.7
  • 8
    • 0019263991 scopus 로고
    • Virus-like particles of yeast
    • Bruenn J. A. Virus-like particles of yeast. Annu. Rev. Microbiol. 34:1980;49-68.
    • (1980) Annu. Rev. Microbiol. , vol.34 , pp. 49-68
    • Bruenn, J.A.1
  • 11
    • 0030924019 scopus 로고    scopus 로고
    • Structure of L-A virus: A specialised compartment for the transcription and replication of double-stranded RNA
    • Caston J. R., Trus B. L., Booy F. P., Wickner R. B., Wall J. S., Steven A. C. Structure of L-A virus: a specialised compartment for the transcription and replication of double-stranded RNA. J. Cell. Biol. 138:1997;975-985.
    • (1997) J. Cell. Biol. , vol.138 , pp. 975-985
    • Caston, J.R.1    Trus, B.L.2    Booy, F.P.3    Wickner, R.B.4    Wall, J.S.5    Steven, A.C.6
  • 13
    • 0021956741 scopus 로고
    • Nucleotide sequence of a yeast Ty1 element: Evidence for an unusual mechanism of gene expression
    • Clare J., Farabaugh P. Nucleotide sequence of a yeast Ty1 element: evidence for an unusual mechanism of gene expression. Proc. Natl Acad. Sci. USA. 82:1985;2829-2833.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 2829-2833
    • Clare, J.1    Farabaugh, P.2
  • 14
    • 1842388680 scopus 로고
    • Efficient translational frameshifting occurs within a conserved sequence of the overlap between the two genes of a yeast Ty1 transposon
    • Clare J. J., Belcourt M., Farabaugh P. J. Efficient translational frameshifting occurs within a conserved sequence of the overlap between the two genes of a yeast Ty1 transposon. Proc. Natl Acad. Sci. USA. 85:1988;6816-6820.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6816-6820
    • Clare, J.J.1    Belcourt, M.2    Farabaugh, P.J.3
  • 15
    • 0030937751 scopus 로고    scopus 로고
    • Visualisation of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J. F., Cheng N., Zlotnik A., Wingfield P. T., Stahl S. J., Steven A. C. Visualisation of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:1997;91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnik, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 16
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R. A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. London ser. B. 261:1971;221-230.
    • (1971) Phil. Trans. Roy. Soc. London Ser. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 17
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R. A., Amos L. A., Finch J. T., DeRosier D. J., Klug A. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature. 226:1970;421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    Derosier, D.J.4    Klug, A.5
  • 18
    • 0028307177 scopus 로고
    • Three-dimensional structure of Hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther R. A., Kiselev N. A., Böttcher B., Berriman J. A., Borisova G. P., Ose V., Pumpens P. Three-dimensional structure of Hepatitis B virus core particles determined by electron cryomicroscopy. Cell. 77:1994;943-950.
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 20
    • 0025771471 scopus 로고
    • Regulation of retrotransposition in Saccharomyces cerevisiae
    • Curcio M. J., Garfinkel D. J. Regulation of retrotransposition in Saccharomyces cerevisiae. Mol. Micobiol. 5:1991a;1823-1829.
    • (1991) Mol. Micobiol. , vol.5 , pp. 1823-1829
    • Curcio, M.J.1    Garfinkel, D.J.2
  • 21
    • 0026082573 scopus 로고
    • Single-step selection for Ty1 element retrotransposition
    • Curcio M. J., Garfinkel D. J. Single-step selection for Ty1 element retrotransposition. Proc. Natl Acad. Sci. USA. 88:1991b;936-940.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 936-940
    • Curcio, M.J.1    Garfinkel, D.J.2
  • 22
    • 0026636672 scopus 로고
    • Post translational control of Ty1 retrotransposition occurs at the level of protein processing
    • Curcio M. J., Garfinkel D. J. Post translational control of Ty1 retrotransposition occurs at the level of protein processing. Mol. Cell. Biol. 12:1992;2813-2825.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2813-2825
    • Curcio, M.J.1    Garfinkel, D.J.2
  • 23
    • 0028222894 scopus 로고
    • Heterogeneous functional Ty1 elements are abundant in the Saccharomyces cerevisiae genome
    • Curcio M. J., Garfinkel D. J. Heterogeneous functional Ty1 elements are abundant in the Saccharomyces cerevisiae genome. Genetics. 136:1994;1245-1259.
    • (1994) Genetics , vol.136 , pp. 1245-1259
    • Curcio, M.J.1    Garfinkel, D.J.2
  • 25
    • 0026579790 scopus 로고
    • Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system
    • Dokland T., Lindqvist B. H., Fuller S. D. Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system. EMBO J. 11:1992;839-846.
    • (1992) EMBO J. , vol.11 , pp. 839-846
    • Dokland, T.1    Lindqvist, B.H.2    Fuller, S.D.3
  • 27
    • 0009902261 scopus 로고
    • RNA from the yeast transposable element Ty1 has both ends in the direct repeats, a structure similar to retrovirus RNA
    • Elder R. T., Loh E. Y., Davis R. W. RNA from the yeast transposable element Ty1 has both ends in the direct repeats, a structure similar to retrovirus RNA. Proc. Natl Acad. Sci. USA. 80:1983;2432-2436.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2432-2436
    • Elder, R.T.1    Loh, E.Y.2    Davis, R.W.3
  • 28
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualisation 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 visualisation of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;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
  • 29
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organised by interactions with a complementary T=3 capsid
    • Fuller S. D. The T=4 envelope of Sindbis virus is organised by interactions with a complementary T=3 capsid. Cell. 48:1987;923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 31
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller S. D., Wilk T., Gowen B. E., Krausslich H. G., Vogt V. M. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7:1997;729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krausslich, H.G.4    Vogt, V.M.5
  • 32
    • 0022129513 scopus 로고
    • Ty element transposition: Reverse transcriptase and virus like particles
    • Garfinkel D. J., Boeke J. D., Fink G. R. Ty element transposition: reverse transcriptase and virus like particles. Cell. 42:1985;507-517.
    • (1985) Cell , vol.42 , pp. 507-517
    • Garfinkel, D.J.1    Boeke, J.D.2    Fink, G.R.3
  • 33
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom H. R. Assembly and morphology of HIV: potential effect of structure on viral function. AIDS. 5:1991;617-638.
    • (1991) AIDS , vol.5 , pp. 617-638
    • Gelderblom, H.R.1
  • 34
    • 0031883282 scopus 로고    scopus 로고
    • Invading the yeast nucleus: A nuclear localization signal at the C terminus of Ty1 integrase is required for transposition in vivo
    • Kenna M. A., Brachmann C. B., Devine S. E., Boeke J. D. Invading the yeast nucleus: a nuclear localization signal at the C terminus of Ty1 integrase is required for transposition in vivo. Mol. Cell Biol. 18:1998;1115-1124.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1115-1124
    • Kenna, M.A.1    Brachmann, C.B.2    Devine, S.E.3    Boeke, J.D.4
  • 35
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B virus core structure: Comparison of human and duck cores
    • Kenney J. M., von Bonsdorff C-H., Nassal M., Fuller S. D. Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure. 3:1995;1009-1019.
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    Von Bonsdorff, C.-H.2    Nassal, M.3    Fuller, S.D.4
  • 36
    • 0024279844 scopus 로고
    • Ty: A retroelement moving forward
    • Kingsman A. J., Kingsman S. M. Ty: a retroelement moving forward. Cell. 53:1988;333-335.
    • (1988) Cell , vol.53 , pp. 333-335
    • Kingsman, A.J.1    Kingsman, S.M.2
  • 38
    • 0029849782 scopus 로고    scopus 로고
    • Identification of proteolytic cleavage sites within the gag analogue protein of Ty1 virus-like particles
    • Martin-Rendon E., Hurd D. W., Marfany G., Kingsman S. M., Kingsman A. J. Identification of proteolytic cleavage sites within the gag analogue protein of Ty1 virus-like particles. Mol. Microbiol. 22:1996b;1035-1043.
    • (1996) Mol. Microbiol. , vol.22 , pp. 1035-1043
    • Martin-Rendon, E.1    Hurd, D.W.2    Marfany, G.3    Kingsman, S.M.4    Kingsman, A.J.5
  • 39
    • 0021933247 scopus 로고
    • A retrovirus-like strategy for the expression of a fusion protein encoded by yeast transposon Ty1
    • Mellor J., Fulton S. M., Dobson M. J., Wilson W., Kingsman S. M., Kingsman A. J. A retrovirus-like strategy for the expression of a fusion protein encoded by yeast transposon Ty1. Nature. 313:1985;243-246.
    • (1985) Nature , vol.313 , pp. 243-246
    • Mellor, J.1    Fulton, S.M.2    Dobson, M.J.3    Wilson, W.4    Kingsman, S.M.5    Kingsman, A.J.6
  • 40
    • 0031883281 scopus 로고    scopus 로고
    • A Ty1 integrase nuclear localisation signal required for transposition
    • Moore S. P., Rinckel L. A., Garfinkel D. J. A Ty1 integrase nuclear localisation signal required for transposition. Mol. Cell Biol. 18:1998;1105-1114.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1105-1114
    • Moore, S.P.1    Rinckel, L.A.2    Garfinkel, D.J.3
  • 41
    • 0023160210 scopus 로고
    • Processing of Ty1 proteins and formation of Ty1 virus-like particles in Saccharomyces cerevisiae
    • Muller F., Bruhl K-H., Friedel K., Kowallik K. V., Ciriacy M. Processing of Ty1 proteins and formation of Ty1 virus-like particles in Saccharomyces cerevisiae. Mol. Gen. Genet. 207:1987;421-442.
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 421-442
    • Muller, F.1    Bruhl, K.-H.2    Friedel, K.3    Kowallik, K.V.4    Ciriacy, M.5
  • 42
    • 0028292220 scopus 로고
    • Fullerene-like organisation of HIV gag-protein shell in virus-like particles produced by recombinant baculovirus
    • Nermut M. V., Hockley D. J., Jowett J. B. M., Jones I. M., Garreau M., Thomas D. Fullerene-like organisation of HIV gag-protein shell in virus-like particles produced by recombinant baculovirus. Virology. 198:1994;288-296.
    • (1994) Virology , vol.198 , pp. 288-296
    • Nermut, M.V.1    Hockley, D.J.2    Jowett, J.B.M.3    Jones, I.M.4    Garreau, M.5    Thomas, D.6
  • 45
    • 0001234868 scopus 로고
    • Yeast RNA virology: The yeast killer systems
    • J. R. Broach, J. R. Pringle, & E. W. Jones. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Wickner R. B. Yeast RNA virology: the yeast killer systems. Broach J. R., Pringle J. R., Jones E. W. Molecular and Cellular Biology of the yeast Saccharomyces cerevisiae. 1991;263-296 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1991) Molecular and Cellular Biology of the Yeast Saccharomyces Cerevisiae , pp. 263-296
    • Wickner, R.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.