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Volumn 218, Issue 1, 1996, Pages 1-13

Mutations in the poliovirus 3CD proteinase S1-specificity pocket affect substrate recognition and RNA binding

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

EID: 0029865104     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0160     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire, M., Chernaia, M. M., Malcolm, B. A., and James, M. N. G. (1994). Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369, 72-76.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.G.4
  • 2
    • 0027170180 scopus 로고
    • Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA
    • Andino, R., Rieckhof, G. E., Achacoso, P. L., and Baltimore, D. (1993). Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12, 3587-3598.
    • (1993) EMBO J. , vol.12 , pp. 3587-3598
    • Andino, R.1    Rieckhof, G.E.2    Achacoso, P.L.3    Baltimore, D.4
  • 3
    • 0025049209 scopus 로고
    • A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA
    • Andino, R., Rieckhof, G. E., and Baltimore, D. (1990a). A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA. Cell 63, 369-380.
    • (1990) Cell , vol.63 , pp. 369-380
    • Andino, R.1    Rieckhof, G.E.2    Baltimore, D.3
  • 4
  • 5
    • 0026094384 scopus 로고
    • Purification, properties, and mutagenesis of poliovirus 3C protease
    • Baum, E. Z., Bebernitz, G. A., Palant, O., Mueller, T., and Plotch, S. J. (1991). Purification, properties, and mutagenesis of poliovirus 3C protease. Virology 185, 140-150.
    • (1991) Virology , vol.185 , pp. 140-150
    • Baum, E.Z.1    Bebernitz, G.A.2    Palant, O.3    Mueller, T.4    Plotch, S.J.5
  • 6
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications
    • Bazan, J. F., and Fletterick, R. J. (1988). Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications. Proc. Natl. Acad. Sci. USA 85, 7872-7876.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 7
    • 0025215061 scopus 로고
    • A mutant poliovirus containing a novel proteolytic cleavage site in VP3 is altered in viral maturation
    • Blair, W. S., Hwang, S.-S., Ypma-Wong, M. F., and Semler, B. L. (1990). A mutant poliovirus containing a novel proteolytic cleavage site in VP3 is altered in viral maturation. J. Virol. 64, 1784-1793.
    • (1990) J. Virol. , vol.64 , pp. 1784-1793
    • Blair, W.S.1    Hwang, S.-S.2    Ypma-Wong, M.F.3    Semler, B.L.4
  • 8
    • 0027405544 scopus 로고
    • A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor
    • Blair, W. S., Li, X., and Semler, B. L. (1993). A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor. J. Virol. 67, 2336-2343.
    • (1993) J. Virol. , vol.67 , pp. 2336-2343
    • Blair, W.S.1    Li, X.2    Semler, B.L.3
  • 9
    • 0025982955 scopus 로고
    • Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase
    • Blair, W. S., and Semler, B. L. (1991). Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase. J. Virol. 65, 6111-6123.
    • (1991) J. Virol. , vol.65 , pp. 6111-6123
    • Blair, W.S.1    Semler, B.L.2
  • 10
    • 0020085040 scopus 로고
    • An SV40 deletion mutant accumulates late transcripts in a paranuclear extract
    • Campos, R., and Villarreal, L. P. (1982). An SV40 deletion mutant accumulates late transcripts in a paranuclear extract. Virology 119, 1-11.
    • (1982) Virology , vol.119 , pp. 1-11
    • Campos, R.1    Villarreal, L.P.2
  • 11
    • 0028065078 scopus 로고
    • Transduction of a human RNA sequence by poliovirus
    • Charini, W. A., Todd, S., Gutman, G. A., and Semler, B. L. (1994). Transduction of a human RNA sequence by poliovirus. J. Virol. 68, 6547-6552.
    • (1994) J. Virol. , vol.68 , pp. 6547-6552
    • Charini, W.A.1    Todd, S.2    Gutman, G.A.3    Semler, B.L.4
  • 12
    • 0010587523 scopus 로고
    • Molecular biology and genetics of poliovirus protein processing
    • B. L. Semler and E. Ehrenfeld, Eds., Am. Soc. Microbiol., Washington, DC
    • Dewalt, P. G., and Semler, B. L. (1989). Molecular biology and genetics of poliovirus protein processing. In "Molecular Aspects of Picornavirus Infection and Detection" (B. L. Semler and E. Ehrenfeld, Eds.), pp. 73-93. Am. Soc. Microbiol., Washington, DC.
    • (1989) Molecular Aspects of Picornavirus Infection and Detection , pp. 73-93
    • Dewalt, P.G.1    Semler, B.L.2
  • 13
    • 0024545738 scopus 로고
    • The deletion of 41 proximal nucleotides reverts a poliovirus mutant containing a temperature-sensitive lesion in the 5′ noncoding region of genomic RNA
    • Dildine, S. L., and Semler, B. L. (1989). The deletion of 41 proximal nucleotides reverts a poliovirus mutant containing a temperature-sensitive lesion in the 5′ noncoding region of genomic RNA. J. Virol. 63, 847-862.
    • (1989) J. Virol. , vol.63 , pp. 847-862
    • Dildine, S.L.1    Semler, B.L.2
  • 14
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W. G., and Semler, B. L. (1993). Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes. Microbiol. Rev. 57, 781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 15
    • 0022570578 scopus 로고
    • Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular serine and cysteine proteinase families
    • Gorbalenya, A. E., Blinov, V. M., and Donchenko, A. P. (1986). Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular serine and cysteine proteinase families. FEBS Lett. 194, 253-257.
    • (1986) FEBS Lett. , vol.194 , pp. 253-257
    • Gorbalenya, A.E.1    Blinov, V.M.2    Donchenko, A.P.3
  • 16
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold
    • Gorbalenya, A. E., Donchenko, A. P., Blinov, V. M., and Koonin, E. V. (1989). Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold. FEBS Lett. 243, 103-114.
    • (1989) FEBS Lett. , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koonin, E.V.4
  • 17
    • 0026766205 scopus 로고
    • Linker scanning mutagenesis of the internal ribosome entry site of poliovirus RNA
    • Haller, A. A., and Semler, B. L. (1992). Linker scanning mutagenesis of the internal ribosome entry site of poliovirus RNA. J. Virol. 66, 5075-5086.
    • (1992) J. Virol. , vol.66 , pp. 5075-5086
    • Haller, A.A.1    Semler, B.L.2
  • 18
    • 0018033878 scopus 로고
    • Complete sequence of constant 3′ noncoding regions of an immunoglobulin mRNA using the dideoxy nucleotide method of RNA sequencing
    • Hamlyn, D. H., Brownlee, G. G., Cheng., C. C., Gait, M. J., and Milstein, C. (1978). Complete sequence of constant 3′ noncoding regions of an immunoglobulin mRNA using the dideoxy nucleotide method of RNA sequencing. Cell 15, 1067-1075.
    • (1978) Cell , vol.15 , pp. 1067-1075
    • Hamlyn, D.H.1    Brownlee, G.G.2    Cheng, C.C.3    Gait, M.J.4    Milstein, C.5
  • 19
    • 0026095274 scopus 로고
    • Site directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase
    • Hammerle, T., Hellen, C. U. T., and Wimmer, E. (1991). Site directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase. J. Biol. Chem. 266, 5412-5416.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5412-5416
    • Hammerle, T.1    Hellen, C.U.T.2    Wimmer, E.3
  • 20
    • 0026744870 scopus 로고
    • Mutational analysis of the proposed FG loop of poliovirus proteinase 3C identifies amino acids that are necessary for 3CD cleavage and might be determinants of a function distinct from proteolytic activity
    • Hammerle, T., Molla, A., and Wimmer, E. (1992). Mutational analysis of the proposed FG loop of poliovirus proteinase 3C identifies amino acids that are necessary for 3CD cleavage and might be determinants of a function distinct from proteolytic activity. J. Virol. 66, 6028-6034.
    • (1992) J. Virol. , vol.66 , pp. 6028-6034
    • Hammerle, T.1    Molla, A.2    Wimmer, E.3
  • 21
    • 0019971712 scopus 로고
    • Proteolytic processing of poliovirus polypeptides: Antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs
    • Hanecak, R., Semler, B. L., Anderson, C. W., and Wimmer, E. (1982). Proteolytic processing of poliovirus polypeptides: Antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc. Natl. Acad. Sci. USA 79, 3973-3977.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3973-3977
    • Hanecak, R.1    Semler, B.L.2    Anderson, C.W.3    Wimmer, E.4
  • 23
    • 0002976376 scopus 로고
    • Oligonucleotide-directed site-specific mutagenesis using double stranded plasmid DNA
    • A. Narang, Ed., Academic Press, New York
    • Inouye, S., and Inouye, M. (1987). Oligonucleotide-directed site-specific mutagenesis using double stranded plasmid DNA. In "Synthesis and Applications of DNA and RNAs" (A. Narang, Ed.), pp. 181-206. Academic Press, New York.
    • (1987) Synthesis and Applications of DNA and RNAs , pp. 181-206
    • Inouye, S.1    Inouye, M.2
  • 24
    • 0004134524 scopus 로고
    • Expression and site-specific mutagenesis of the poliovirus 3c protease in Escherichia coli
    • Ivanoff, L. A., Towatari, T., Ray, J., Korant, B. D., and Petteway, S. R. (1986). Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 5392-5396.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5392-5396
    • Ivanoff, L.A.1    Towatari, T.2    Ray, J.3    Korant, B.D.4    Petteway, S.R.5
  • 25
    • 0023952330 scopus 로고
    • Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro
    • Jore, J., De Geus, B., Jackson, R. J., Pouwels, P. H., and Enger-Valk, B. E. (1988). Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro. J. Gen. Virol. 69, 1627-1636.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1627-1636
    • Jore, J.1    De Geus, B.2    Jackson, R.J.3    Pouwels, P.H.4    Enger-Valk, B.E.5
  • 26
    • 0027291014 scopus 로고
    • Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites
    • Kean, K. M., Howell, M. T., Grunert, S., Girard, M., and Jackson, R. J. (1993). Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites. Virology 194, 360-364.
    • (1993) Virology , vol.194 , pp. 360-364
    • Kean, K.M.1    Howell, M.T.2    Grunert, S.3    Girard, M.4    Jackson, R.J.5
  • 27
    • 0025752334 scopus 로고
    • Analysis of putative active site residues of the poliovirus 3C protease
    • Kean, K. M., Teterina, N. L., Marc, D., and Girard, M. (1991). Analysis of putative active site residues of the poliovirus 3C protease. Virology 181, 609-619.
    • (1991) Virology , vol.181 , pp. 609-619
    • Kean, K.M.1    Teterina, N.L.2    Marc, D.3    Girard, M.4
  • 29
    • 0025127911 scopus 로고
    • Species-specific substrate interaction of picornavirus 3C proteinase suballelic exchange mutants
    • Lawson, M. A., Dasmahapatra, B., and Semler, B. L. (1990). Species-specific substrate interaction of picornavirus 3C proteinase suballelic exchange mutants. J. Biol. Chem. 265, 15920-15931.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15920-15931
    • Lawson, M.A.1    Dasmahapatra, B.2    Semler, B.L.3
  • 30
    • 0025721937 scopus 로고
    • Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad
    • Lawson, M. A., and Semler, B. L. (1991). Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad. Proc. Natl. Acad. Sci. USA 88, 9919-9923.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9919-9923
    • Lawson, M.A.1    Semler, B.L.2
  • 31
    • 0027500787 scopus 로고
    • pro) binds specifically to the 5′-noncoding region of the viral RNA
    • pro) binds specifically to the 5′-noncoding region of the viral RNA. J. Biol. Chem. 268, 25735-25739.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25735-25739
    • Leong, L.E.-C.1    Walker, P.A.2    Porter, A.G.3
  • 32
    • 0025782267 scopus 로고
    • Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails
    • Lilius, G., Persson, M., Bülow, L., and Mosbach, K. (1991). Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails. Eur. J. Biochem. 198, 499-504.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 499-504
    • Lilius, G.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 34
    • 84966189563 scopus 로고
    • Proteolytic processing in the replication of polio and related viruses
    • Nicklin, M. J. H., Toyoda, H., Murray, M. G., and Wimmer, E. (1986). Proteolytic processing in the replication of polio and related viruses. Biotechnology 4, 36-42.
    • (1986) Biotechnology , vol.4 , pp. 36-42
    • Nicklin, M.J.H.1    Toyoda, H.2    Murray, M.G.3    Wimmer, E.4
  • 37
    • 0023123775 scopus 로고
    • Site-specific mutagenesis of cDNA clones expressing a poliovirus proteinase
    • Semler, B. L., Johnson, V. H., Dewalt, P. G., and Ypma-Wong, M. F. (1987). Site-specific mutagenesis of cDNA clones expressing a poliovirus proteinase. J. Cell. Biochem. 33, 39-51
    • (1987) J. Cell. Biochem. , vol.33 , pp. 39-51
    • Semler, B.L.1    Johnson, V.H.2    Dewalt, P.G.3    Ypma-Wong, M.F.4
  • 38
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography
    • Smith, M. C., Furman, T. C., Ingolia, T. D., and Pidgeon, C. (1988). Chelating peptide-immobilized metal ion affinity chromatography. J. Biol. Chem. 263, 7211-7215.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Furman, T.C.2    Ingolia, T.D.3    Pidgeon, C.4
  • 39
    • 0023043280 scopus 로고
    • A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
    • Toyoda, H., Nicklin, M. J. H., Murray, M. G., Anderson, C. W., Dunn, J. J., Studier, F. W., and Wimmer, E. (1986). A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein. Cell 45, 761-770.
    • (1986) Cell , vol.45 , pp. 761-770
    • Toyoda, H.1    Nicklin, M.J.H.2    Murray, M.G.3    Anderson, C.W.4    Dunn, J.J.5    Studier, F.W.6    Wimmer, E.7
  • 40
    • 0013815610 scopus 로고
    • Infectious poliovirus RNA: A sensitive method of assay
    • Vaheri, A., and Pagano, J. S. (1965). Infectious poliovirus RNA: A sensitive method of assay. Virology 27, 435-436.
    • (1965) Virology , vol.27 , pp. 435-436
    • Vaheri, A.1    Pagano, J.S.2
  • 42
    • 0029061499 scopus 로고
    • Sequence and structural determinants of the interaction between the 5′-noncoding region of picornavirus RNA and rhinovirus protease 3C
    • Walker, P. A., Leong, L. E.-C., and Porter, A. G. (1995). Sequence and structural determinants of the interaction between the 5′-noncoding region of picornavirus RNA and rhinovirus protease 3C. J. Biol. Chem. 270, 14510-14516.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14510-14516
    • Walker, P.A.1    Leong, L.E.-C.2    Porter, A.G.3
  • 44
    • 0023650625 scopus 로고
    • In vitro molecular genetics as a tool for determining the differential cleavage specificities of the poliovirus 3C proteinase
    • Ypma-Wong, M. F., and Semler, B. L. (1987a). In vitro molecular genetics as a tool for determining the differential cleavage specificities of the poliovirus 3C proteinase. Nucleic Acids Res. 15, 2069-2088.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 2069-2088
    • Ypma-Wong, M.F.1    Semler, B.L.2
  • 45
    • 0023224697 scopus 로고
    • Processing determinants required for in vitro cleavage of the poliovirus p1 precursor to capsid proteins
    • Ypma-Wong, M. F., and Semler, B. L. (1987b). Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins. J. Virol. 61, 3181-3189.
    • (1987) J. Virol. , vol.61 , pp. 3181-3189
    • Ypma-Wong, M.F.1    Semler, B.L.2
  • 46
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 precursor
    • Ypma-Wong, M. F., Dewalt, P. G., Johnson, V. H., Lamb, J. G., and Semler, B. L. (1988a). Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 precursor. Virology 166, 265-270.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.L.5
  • 47
    • 0024297314 scopus 로고
    • Structural domains of the poliovirus polyprotein are major determinants for proteolytic cleavage at gln-gly pairs
    • Ypma-Wong, M. F., Filman, D. J., Hogle, J. M., and Semler, B. L. (1988b). Structural domains of the poliovirus polyprotein are major determinants for proteolytic cleavage at gln-gly pairs. J. Biol. Chem. 63, 17846-17856.
    • (1988) J. Biol. Chem. , vol.63 , pp. 17846-17856
    • Ypma-Wong, M.F.1    Filman, D.J.2    Hogle, J.M.3    Semler, B.L.4


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