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Volumn 17, Issue 1, 1999, Pages 128-138

Production of 'authentic' poliovirus RNA-dependent RNA polymerase (3D(pol)) by ubiquitin-protease-mediated cleavage in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CODON; DEFORMYLASE; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENE EXPRESSION SYSTEM; METHIONINE AMINOPEPTIDASE; POLIOMYELITIS VIRUS; PROTEINASE; RNA POLYMERASE; UBIQUITIN; VIRUS RNA;

EID: 0033212780     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1100     Document Type: Article
Times cited : (122)

References (23)
  • 1
    • 0030332528 scopus 로고    scopus 로고
    • Comparison of the replication of positive-stranded RNA viruses of plants and animals
    • Buck K. W. Comparison of the replication of positive-stranded RNA viruses of plants and animals. Adv. Virus Res. 47:1996;159-251.
    • (1996) Adv. Virus Res. , vol.47 , pp. 159-251
    • Buck, K.W.1
  • 2
    • 0000126962 scopus 로고    scopus 로고
    • Enteroviruses: Polioviruses, coxsackieviruses, echoviruses and new enteroviruses
    • B. N. Fields, D. M. Knipe, & P. M. Howley. Philadelphia: Lippincott-Raven
    • Melnick J. L. Enteroviruses: Polioviruses, coxsackieviruses, echoviruses and new enteroviruses. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;669-670 Lippincott-Raven, Philadelphia.
    • (1996) Fields Virology , pp. 669-670
    • Melnick, J.L.1
  • 5
    • 0025758176 scopus 로고
    • Expression and characterization of poliovirus proteins 3BVPg, 3Cpro, and 3Dpol in recombinant baculovirus-infected Spodoptera frugiperda cells
    • Neufeld K. L., Richards O. C., Ehrenfeld E. Expression and characterization of poliovirus proteins 3BVPg, 3Cpro, and 3Dpol in recombinant baculovirus-infected Spodoptera frugiperda cells. Virus. Res. 19:1991;173-188.
    • (1991) Virus. Res. , vol.19 , pp. 173-188
    • Neufeld, K.L.1    Richards, O.C.2    Ehrenfeld, E.3
  • 6
    • 0026325741 scopus 로고
    • Purification, characterization, and comparison of poliovirus RNA polymerase from native and recombinant sources
    • Neufeld K. L., Richards O. C., Ehrenfeld E. Purification, characterization, and comparison of poliovirus RNA polymerase from native and recombinant sources. J. Biol. Chem. 266:1991;24212-24219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24212-24219
    • Neufeld, K.L.1    Richards, O.C.2    Ehrenfeld, E.3
  • 7
    • 0024495371 scopus 로고
    • Purification and properties of poliovirus RNA polymerase expressed in Escherichia coli
    • Plotch S. J., Palant O., Gluzman Y. Purification and properties of poliovirus RNA polymerase expressed in Escherichia coli. J. Virol. 63:1989;216-225.
    • (1989) J. Virol. , vol.63 , pp. 216-225
    • Plotch, S.J.1    Palant, O.2    Gluzman, Y.3
  • 8
    • 0030696625 scopus 로고    scopus 로고
    • Purification, characterization, and inhibition of peptide deformylase from Escherichia coli
    • Rajagopalan P. T., Datta A., Pei D. Purification, characterization, and inhibition of peptide deformylase from Escherichia coli. Biochemistry. 36:1997;13910-13918.
    • (1997) Biochemistry , vol.36 , pp. 13910-13918
    • Rajagopalan, P.T.1    Datta, A.2    Pei, D.3
  • 9
    • 0023135722 scopus 로고
    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • Ben-Bassat A., Bauer K., Chang S. Y., Myambo K., Boosman A., Chang S. Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169:1987;751-757.
    • (1987) J. Bacteriol. , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 10
    • 0029065387 scopus 로고
    • Improved amino-terminal processing of recombinant proteins synthesized in Escherichia coli
    • Sandman K., Grayling R. A., Reeve J. N. Improved amino-terminal processing of recombinant proteins synthesized in Escherichia coli. Biotechnology. 13:1995;504-506.
    • (1995) Biotechnology , vol.13 , pp. 504-506
    • Sandman, K.1    Grayling, R.A.2    Reeve, J.N.3
  • 11
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen J. L., Long A. M., Schultz S. C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure. 5:1997;1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 12
    • 0029870896 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant human Theta-class glutathione transferase (GSTT2-2)
    • Tan K. L., Board P. G. Purification and characterization of a recombinant human Theta-class glutathione transferase (GSTT2-2). Biochem. J. 315:1996;727-732.
    • (1996) Biochem. J. , vol.315 , pp. 727-732
    • Tan, K.L.1    Board, P.G.2
  • 13
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker R. T., Tobias J. W., Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem. 267:1992;23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 14
    • 0003903343 scopus 로고
    • (, Irwin, N, Ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J, Fritsch, E. F, and, Maniatis, T. 1989, Molecular Cloning, (, Irwin, N, Ed.), Vol, 1, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning , vol.1
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 15
    • 0029682812 scopus 로고    scopus 로고
    • Site-directed mutagenesis using overlap extension PCR
    • Aiyar A., Xiang Y., Leis J. Site-directed mutagenesis using overlap extension PCR. Methods Mol. Biol. 57:1996;177-191.
    • (1996) Methods Mol. Biol. , vol.57 , pp. 177-191
    • Aiyar, A.1    Xiang, Y.2    Leis, J.3
  • 16
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae
    • Tobias J. W., Varshavsky A. Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. J. Biol. Chem. 266:1991;12021-12028.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 18
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 19
    • 0028152526 scopus 로고
    • Studies with poliovirus polymerase 3Dpol. Stimulation of poly(U) synthesis in vitro by purified poliovirus protein 3AB
    • Paul A. V., Cao X., Harris K. S., Lama J., Wimmer E. Studies with poliovirus polymerase 3Dpol. Stimulation of poly(U) synthesis in vitro by purified poliovirus protein 3AB. J. Biol. Chem. 269:1994;29173-29181.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29173-29181
    • Paul, A.V.1    Cao, X.2    Harris, K.S.3    Lama, J.4    Wimmer, E.5
  • 20
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus- And plus-strand RNA synthesis
    • Lemm J. A., Rumenapf T., Strauss E. G., Strauss J. H., Rice C. M. Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus- and plus-strand RNA synthesis. EMBO J. 13:1994;2925-2934.
    • (1994) EMBO J. , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rumenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 21
    • 0028142992 scopus 로고
    • Protein expression using cotranslational fusion and cleavage of ubiquitin. Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase
    • Baker R. T., Smith S. A., Marano R., McKee J., Board P. G. Protein expression using cotranslational fusion and cleavage of ubiquitin. Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase. J. Biol. Chem. 269:1994;25381-25386.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25381-25386
    • Baker, R.T.1    Smith, S.A.2    Marano, R.3    McKee, J.4    Board, P.G.5
  • 22
    • 0030131709 scopus 로고    scopus 로고
    • High-level expression and efficient recovery of ubiquitin fusion proteins from Escherichia coli
    • Pilon A. L., Yost P., Chase T. E., Lohnas G. L., Bentley W. E. High-level expression and efficient recovery of ubiquitin fusion proteins from Escherichia coli. Biotechnol. Prog. 12:1996;331-337.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 331-337
    • Pilon, A.L.1    Yost, P.2    Chase, T.E.3    Lohnas, G.L.4    Bentley, W.E.5
  • 23
    • 0029330222 scopus 로고
    • Functional oligomerization of poliovirus RNA-dependent RNA polymerase
    • Pata J. D., Schultz S. C., Kirkegaard K. Functional oligomerization of poliovirus RNA-dependent RNA polymerase. RNA. 1:1995;466-477.
    • (1995) RNA , vol.1 , pp. 466-477
    • Pata, J.D.1    Schultz, S.C.2    Kirkegaard, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.