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Volumn 300, Issue 1, 2002, Pages 60-70

New targets for antivirals: The ribosomal A-site and the factors that interact with it

Author keywords

Drugs; Elongation factors; Frameshifting; HIV; Ribosome; Translation; Virus

Indexed keywords

ANISOMYCIN; ANTIVIRUS AGENT; ELONGATION FACTOR; PREUSSIN; SORDARIN;

EID: 0036383052     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2002.1567     Document Type: Article
Times cited : (49)

References (36)
  • 1
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
    • al Karadaghi, S., Aevarsson, A., Garber, M., Zheltonosova, J., and Liljas, A. (1996). The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange. Structure 4, 555-565.
    • (1996) Structure , vol.4 , pp. 555-565
    • Al Karadaghi, S.1    Aevarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 2
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha
    • Andersen, G. R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T. G., Kjeldgaard, M., and Nyborg, J. (2000). Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol. Cell 6, 1261-1266.
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 3
    • 0035005341 scopus 로고    scopus 로고
    • Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex
    • Andersen, G. R., Valente, L., Pedersen, L., Kinzy, T. G., and Nyborg, J. (2001). Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex. Nat. Struct. Biol. 8, 531-534.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 531-534
    • Andersen, G.R.1    Valente, L.2    Pedersen, L.3    Kinzy, T.G.4    Nyborg, J.5
  • 4
    • 0029091681 scopus 로고
    • Ribosomal frameshifting on viral RNAs
    • Brierley, I. (1995). Ribosomal frameshifting on viral RNAs. J. Gen. Virol. 76, 1885-1892.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1885-1892
    • Brierley, I.1
  • 5
    • 0033569767 scopus 로고    scopus 로고
    • Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange
    • Carr-Schmid, A., Durko, N., Cavallius, J., Merrick, W. C., and Kinzy, T. G. (1999). Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange. J. Biol. Chem. 274, 30297-30302.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30297-30302
    • Carr-Schmid, A.1    Durko, N.2    Cavallius, J.3    Merrick, W.C.4    Kinzy, T.G.5
  • 6
    • 0032788546 scopus 로고    scopus 로고
    • Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity
    • Carr-Schmid, A., Valente, L., Loik, V. I., Williams, T., Starita, L. M., and Kinzy, T. G. (1999). Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity. Mol. Cell. Biol. 19, 5257-5266.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5257-5266
    • Carr-Schmid, A.1    Valente, L.2    Loik, V.I.3    Williams, T.4    Starita, L.M.5    Kinzy, T.G.6
  • 7
    • 0015877247 scopus 로고
    • The tricodermin group of antibiotics, inhibitors of peptide bond formation by eukaryotic ribosomes
    • Carrasco, L., Barbacid, M., and Vazquez, D. (1973). The tricodermin group of antibiotics, inhibitors of peptide bond formation by eukaryotic ribosomes. Biochim. Biophys. Acta 312, 368-376.
    • (1973) Biochim. Biophys. Acta , vol.312 , pp. 368-376
    • Carrasco, L.1    Barbacid, M.2    Vazquez, D.3
  • 8
    • 0032582798 scopus 로고    scopus 로고
    • Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered nucleotide specificity
    • Cavallius, J., and Merrick, W. C. (1998). Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered nucleotide specificity. J. Biol. Chem. 273, 28752-28758.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28752-28758
    • Cavallius, J.1    Merrick, W.C.2
  • 9
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski, J., Wang, J., Steitz, T. A., and Moore, P. B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 10
    • 0026098002 scopus 로고
    • A -1 ribosomal frameshift in a double-stranded RNA virus forms a gag-pol fusion protein
    • Dinman, J. D., Icho, T., and Wickner, R. B. (1991). A 31 ribosomal frameshift in a double-stranded RNA virus forms a gag-pol fusion protein. Proc. Natl. Acad. Sci. USA 88, 174-178.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 174-178
    • Dinman, J.D.1    Icho, T.2    Wickner, R.B.3
  • 11
    • 0030817938 scopus 로고    scopus 로고
    • Translational misreading: Mutations in translation elongation factor 1α differentially affect programmed ribosomal frameshifting and drug sensitivity
    • Dinman, J. D., and Kinzy, T. G. (1997). Translational misreading: Mutations in translation elongation factor 1α differentially affect programmed ribosomal frameshifting and drug sensitivity. RNA 3, 870-881.
    • (1997) RNA , vol.3 , pp. 870-881
    • Dinman, J.D.1    Kinzy, T.G.2
  • 12
    • 0030966221 scopus 로고    scopus 로고
    • Peptidyl transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: Development of model systems
    • Dinman, J. D., Ruiz-Echevarria, M. J., Czaplinski, K., and Peltz, S. W. (1997). Peptidyl transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: Development of model systems. Proc. Natl. Acad. Sci. USA 94, 6606-6611.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6606-6611
    • Dinman, J.D.1    Ruiz-Echevarria, M.J.2    Czaplinski, K.3    Peltz, S.W.4
  • 13
    • 0032054710 scopus 로고    scopus 로고
    • Translating old drugs into new treatments: Identifying compounds that modulate programmed -1 ribosomal frameshifting and function as potential antiviral agents
    • Dinman, J. D., Ruiz-Echevarria, M. J., and Peltz, S. W. (1998). Translating old drugs into new treatments: Identifying compounds that modulate programmed -1 ribosomal frameshifting and function as potential antiviral agents. Trends Biotechniques 16, 190-196.
    • (1998) Trends Biotechniques , vol.16 , pp. 190-196
    • Dinman, J.D.1    Ruiz-Echevarria, M.J.2    Peltz, S.W.3
  • 14
    • 0028032017 scopus 로고
    • Translational maintenance of frame: Mutants of Saccharomyces cerevisiae with altered -1 ribosomal frameshifting efficiencies
    • Dinman, J. D., and Wickner, R. B. (1994). Translational maintenance of frame: Mutants of Saccharomyces cerevisiae with altered -1 ribosomal frameshifting efficiencies. Genetics 136, 75-86.
    • (1994) Genetics , vol.136 , pp. 75-86
    • Dinman, J.D.1    Wickner, R.B.2
  • 15
    • 0033529540 scopus 로고    scopus 로고
    • Sordarin inhibits fungal protein synthesis by blocking translocation differently to fusidic acid
    • Dominguez, J. M., Gomez-Lorenzo, M. G., and Martin, J. J. (1999). Sordarin inhibits fungal protein synthesis by blocking translocation differently to fusidic acid. J. Biol. Chem. 274, 22423-22427.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22423-22427
    • Dominguez, J.M.1    Gomez-Lorenzo, M.G.2    Martin, J.J.3
  • 16
    • 0029870925 scopus 로고    scopus 로고
    • Programmed translational frameshifting
    • Farabaugh, P. J. (1996). Programmed translational frameshifting. Microbiol. Rev. 60, 103-134.
    • (1996) Microbiol. Rev. , vol.60 , pp. 103-134
    • Farabaugh, P.J.1
  • 17
    • 0014198715 scopus 로고
    • Inhibitors of protein biosynthesis. II. Mode of action of anisomycin
    • Grollman, A. P. (1967). Inhibitors of protein biosynthesis. II. Mode of action of anisomycin. J. Biol. Chem. 242, 3226-3233.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3226-3233
    • Grollman, A.P.1
  • 18
    • 0035919680 scopus 로고    scopus 로고
    • Ty1 retrotransposition and programmed -1 ribosomal frameshifting require the integrity of the protein synthetic translocation step
    • Harger, J. W., Meskauskas, A., Nielsen, N., Justice, M. C., and Dinman, J. D. (2001). Ty1 retrotransposition and programmed -1 ribosomal frameshifting require the integrity of the protein synthetic translocation step. Virology 286, 216-224.
    • (2001) Virology , vol.286 , pp. 216-224
    • Harger, J.W.1    Meskauskas, A.2    Nielsen, N.3    Justice, M.C.4    Dinman, J.D.5
  • 19
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 20
    • 0024277965 scopus 로고
    • Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region
    • Jacks, T., Madhani, H. D., Masiraz, F. R., and Varmus, H. E. (1988). Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region. Cell 55, 447-458.
    • (1988) Cell , vol.55 , pp. 447-458
    • Jacks, T.1    Madhani, H.D.2    Masiraz, F.R.3    Varmus, H.E.4
  • 21
    • 0032488918 scopus 로고    scopus 로고
    • Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis
    • Justice, M. C., Hsu, M. J., Tse, B., Ku, T., Balkovec, J., Schmatz, D., and Nielsen, J. (1998). Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J. Biol. Chem. 273, 3148-3151.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3148-3151
    • Justice, M.C.1    Hsu, M.J.2    Tse, B.3    Ku, T.4    Balkovec, J.5    Schmatz, D.6    Nielsen, J.7
  • 22
    • 0001298958 scopus 로고    scopus 로고
    • Nontranslational functions of components of the translational apparatus
    • N. Sonenberg, J. W. B. Hershey, and M. B. Mathews, Eds. Cold Spring Harbor Press, Cold Spring Harbor, NY
    • Kinzy, T. G., and Goldman, E. (2000). Nontranslational functions of components of the translational apparatus. In "Translational Control of Gene Expression" (N. Sonenberg, J. W. B. Hershey, and M. B. Mathews, Eds.), Vol. 39, pp. 973-997. Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , vol.39 , pp. 973-997
    • Kinzy, T.G.1    Goldman, E.2
  • 23
    • 0029082112 scopus 로고
    • Increased expression of Saccharomyces cerevisiae translation elongation factor 1 alpha bypasses the lethality of a TEF5 null allele encoding elongation factor 1 beta
    • Kinzy, T. G., and Woolford, J. L., Jr. (1995). Increased expression of Saccharomyces cerevisiae translation elongation factor 1 alpha bypasses the lethality of a TEF5 null allele encoding elongation factor 1 beta. Genetics 141, 481-489.
    • (1995) Genetics , vol.141 , pp. 481-489
    • Kinzy, T.G.1    Woolford J.L., Jr.2
  • 24
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996). MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 25
    • 0033989089 scopus 로고    scopus 로고
    • Improved purification of the double-stranded RNA from killer strains of yeast
    • Liermann, R. T., Dinman, J. D., Sylvers, L. A., and Jackson, J. C. (2000). Improved purification of the double-stranded RNA from killer strains of yeast. Biotechniques 28, 64-65.
    • (2000) Biotechniques , vol.28 , pp. 64-65
    • Liermann, R.T.1    Dinman, J.D.2    Sylvers, L.A.3    Jackson, J.C.4
  • 26
    • 0002024553 scopus 로고    scopus 로고
    • The protein biosynthesis elongation cycle
    • N. Sonenberg, J. W. B. Hershey, and M. B. Mathews, Eds. Cold Spring Harbor Press, Cold Spring Harbor, NY
    • Merrick, W. C., and Nyborg, J. (2000). The protein biosynthesis elongation cycle. In "Translational Control of Gene Expression" (N. Sonenberg, J. W. B. Hershey, and M. B. Mathews, Eds.), Vol. 39, pp. 89-126. Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , vol.39 , pp. 89-126
    • Merrick, W.C.1    Nyborg, J.2
  • 27
    • 0034897729 scopus 로고    scopus 로고
    • Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae
    • Meskauskas, A., and Dinman, J. D. (2001). Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae. RNA. 7, 1084-1096.
    • (2001) RNA , vol.7 , pp. 1084-1096
    • Meskauskas, A.1    Dinman, J.D.2
  • 29
    • 0030970289 scopus 로고    scopus 로고
    • Ribosomes and translation
    • Noller, H. F. (1997). Ribosomes and translation. Annu. Rev. Biochem. 66, 679-716.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 679-716
    • Noller, H.F.1
  • 30
    • 0000163138 scopus 로고
    • N. Ford, C. Nolan, and M. Ferguson, Eds., Cold Spring Harbor Press, Cold Spring Harbor, NY
    • Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). "Molecular Cloning, A Laboratory Manual" (N. Ford, C. Nolan, and M. Ferguson, Eds.), Vol. 2(1), Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning, A Laboratory Manual , vol.2 , Issue.1
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 31
    • 0024229383 scopus 로고
    • Mutations in elongation factor EF-1α affect the frequency of frameshifting and amino acid misincorporation in Saccharomyces cerevisiae
    • Sandbaken, M. G., and Culbertson, M. R. (1988). Mutations in elongation factor EF-13 affect the frequency of frameshifting and amino acid misincorporation in Saccharomyces cerevisiae. Genetics 120, 923-934.
    • (1988) Genetics , vol.120 , pp. 923-934
    • Sandbaken, M.G.1    Culbertson, M.R.2
  • 33
    • 0031883153 scopus 로고    scopus 로고
    • Pokeweed antiviral protein specifically inhibits Ty1 directed +1 ribosomal frameshifting and Ty1 retrotransposition in Saccharomyces cerevisiae
    • Tumer, N. E., Parikh, B., Li, P., and Dinman, J. D. (1998). Pokeweed antiviral protein specifically inhibits Ty1 directed 31 ribosomal frameshifting and Ty1 retrotransposition in Saccharomyces cerevisiae. J. Virol. 72, 1036-1042.
    • (1998) J. Virol. , vol.72 , pp. 1036-1042
    • Tumer, N.E.1    Parikh, B.2    Li, P.3    Dinman, J.D.4
  • 34
    • 0010553590 scopus 로고    scopus 로고
    • UNAIDS/WHO Global AIDS Statistics. (2001). AIDS Care 13, 408.
    • (2001) AIDS Care , vol.13 , pp. 408
  • 35
    • 0030443751 scopus 로고    scopus 로고
    • Prions and RNA viruses of Saccharomyces cerevisiae
    • Wickner, R. B. (1996). Prions and RNA viruses of Saccharomyces cerevisiae. Ann. Rev. Genet. 30, 109-139.
    • (1996) Ann. Rev. Genet. , vol.30 , pp. 109-139
    • Wickner, R.B.1
  • 36
    • 0017295312 scopus 로고
    • Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae
    • Wickner, R. B., and Leibowitz, M. J. (1976). Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae. Genetics 82, 429-442.
    • (1976) Genetics , vol.82 , pp. 429-442
    • Wickner, R.B.1    Leibowitz, M.J.2


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