메뉴 건너뛰기




Volumn 71, Issue 3, 1997, Pages 2182-2191

Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein λ1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CAPSID PROTEIN; CORE PROTEIN; NUCLEOSIDE TRIPHOSPHATASE;

EID: 0031055059     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.3.2182-2191.1997     Document Type: Article
Times cited : (61)

References (46)
  • 1
    • 0019999992 scopus 로고
    • Sequences at both termini of the 10 genes of reovirus serotype 3 (strain Dearing)
    • Antczak, J. B., R. Chmelo, D. J. Pickup, and W. K. Joklik. 1982. Sequences at both termini of the 10 genes of reovirus serotype 3 (strain Dearing). Virology 121:307-319.
    • (1982) Virology , vol.121 , pp. 307-319
    • Antczak, J.B.1    Chmelo, R.2    Pickup, D.J.3    Joklik, W.K.4
  • 2
    • 0015213565 scopus 로고
    • Initiation of reovirus mRNA synthesis in vitro
    • Banerjee, A. K., R. Ward, and A. J. Shatkin. 1971. Initiation of reovirus mRNA synthesis in vitro. Nature New Biol. 230:169-172.
    • (1971) Nature New Biol. , vol.230 , pp. 169-172
    • Banerjee, A.K.1    Ward, R.2    Shatkin, A.J.3
  • 3
    • 0024110653 scopus 로고
    • The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1
    • Bartlett, J. A., and W. K. Joklik. 1988. The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1. Virology 167:31-37.
    • (1988) Virology , vol.167 , pp. 31-37
    • Bartlett, J.A.1    Joklik, W.K.2
  • 4
    • 0014838436 scopus 로고
    • Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus
    • Borsa, J., J. Grover, and J. D. Chapman. 1970. Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus. J. Virol. 6:295-302.
    • (1970) J. Virol. , vol.6 , pp. 295-302
    • Borsa, J.1    Grover, J.2    Chapman, J.D.3
  • 5
    • 0015827479 scopus 로고
    • New intermediate subviral particles in the in vitro uncoating of reovirus virions by chymotrypsin
    • Borsa, J., T. P. Copps, M. D. Sargent, D. G. Long, and J. D. Chapman. 1973. New intermediate subviral particles in the in vitro uncoating of reovirus virions by chymotrypsin. J. Virol. 11:552-564.
    • (1973) J. Virol. , vol.11 , pp. 552-564
    • Borsa, J.1    Copps, T.P.2    Sargent, M.D.3    Long, D.G.4    Chapman, J.D.5
  • 6
    • 0015576795 scopus 로고
    • Extraordinary effects of specific monovalent cations on activation of reovirus transcriptase by chymotrypsin in vitro
    • Borsa, J., M. D. Sargent, D. G. Long, and J. D. Chapman. 1973. Extraordinary effects of specific monovalent cations on activation of reovirus transcriptase by chymotrypsin in vitro. J. Virol. 11:207-217.
    • (1973) J. Virol. , vol.11 , pp. 207-217
    • Borsa, J.1    Sargent, M.D.2    Long, D.G.3    Chapman, J.D.4
  • 7
  • 8
    • 0022478937 scopus 로고
    • Reovirus guanylyltransferase is L2 gene product lambda 2
    • Cleveland, D. R., H. Zarbl, and S. Millward. 1986. Reovirus guanylyltransferase is L2 gene product lambda 2. J. Virol. 60:307-311.
    • (1986) J. Virol. , vol.60 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 9
    • 0025003413 scopus 로고
    • Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein
    • Coombs, K. M., B. N. Fields, and S. C. Harrison. 1990. Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein. J. Mol. Biol. 215:1-5.
    • (1990) J. Mol. Biol. , vol.215 , pp. 1-5
    • Coombs, K.M.1    Fields, B.N.2    Harrison, S.C.3
  • 10
    • 0020079241 scopus 로고
    • Activation and characterization of the reovirus transcriptase: Genetic analysis
    • Drayna, D., and B. N. Fields. 1982. Activation and characterization of the reovirus transcriptase: genetic analysis. J. Virol. 41:110-118.
    • (1982) J. Virol. , vol.41 , pp. 110-118
    • Drayna, D.1    Fields, B.N.2
  • 11
    • 0025320720 scopus 로고
    • Active site localization in a viral mRNA capping enzyme
    • Fausnaugh, J., and A. J. Shatkin. 1990. Active site localization in a viral mRNA capping enzyme. J. Biol. Chem. 265:7669-7672.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7669-7672
    • Fausnaugh, J.1    Shatkin, A.J.2
  • 12
    • 0023945392 scopus 로고
    • Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles
    • Furlong, D. B., M. L. Nibert, and B. N. Fields. 1988. Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles. J. Virol. 62:246-256.
    • (1988) J. Virol. , vol.62 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 14
    • 0028352861 scopus 로고
    • Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II
    • Goodrich, J. A., and R. Tjian. 1994. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell 77: 145-156.
    • (1994) Cell , vol.77 , pp. 145-156
    • Goodrich, J.A.1    Tjian, R.2
  • 15
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A. E., and E. V. Koonin. 1993. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3:419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 16
    • 0029079703 scopus 로고
    • Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase
    • Gross, C. H., and S. Shuman. 1995. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase. J. Virol. 69:4727-4736.
    • (1995) J. Virol. , vol.69 , pp. 4727-4736
    • Gross, C.H.1    Shuman, S.2
  • 17
    • 0030050636 scopus 로고    scopus 로고
    • The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding
    • Gross, C. H., and S. Shuman. 1996. The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding. J. Virol. 70:1706-1713.
    • (1996) J. Virol. , vol.70 , pp. 1706-1713
    • Gross, C.H.1    Shuman, S.2
  • 18
    • 0014965713 scopus 로고
    • Four base-specific nucleoside 5′-triphosphatases in the subviral core of reovirus
    • Kapuler, A. M., N. Mendelsohn, H. Klett, and G. Acs. 1970. Four base-specific nucleoside 5′-triphosphatases in the subviral core of reovirus. Nature 225:1209-1213.
    • (1970) Nature , vol.225 , pp. 1209-1213
    • Kapuler, A.M.1    Mendelsohn, N.2    Klett, H.3    Acs, G.4
  • 19
    • 0027474037 scopus 로고
    • Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus
    • Koonin, E. V. 1993. Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus. J. Gen. Virol. 74:733-740.
    • (1993) J. Gen. Virol. , vol.74 , pp. 733-740
    • Koonin, E.V.1
  • 20
    • 0000207228 scopus 로고
    • Evolution of double-stranded RNA viruses: A case for polyphyletic origin from different groups of positive-stranded RNA viruses
    • Koonin, E. V. 1992. Evolution of double-stranded RNA viruses: a case for polyphyletic origin from different groups of positive-stranded RNA viruses. Semin. Virol. 3:327-340.
    • (1992) Semin. Virol. , vol.3 , pp. 327-340
    • Koonin, E.V.1
  • 21
    • 0028173555 scopus 로고
    • Reovirus lambda 1 protein: Affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif
    • Lemay, G., and C. Danis. 1994. Reovirus lambda 1 protein: affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif. J. Gen. Virol. 75:3261-3266.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3261-3266
    • Lemay, G.1    Danis, C.2
  • 22
    • 0025947194 scopus 로고
    • Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase
    • Mao, Z. X., and W. K. Joklik. 1991. Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase. Virology 185:377-386.
    • (1991) Virology , vol.185 , pp. 377-386
    • Mao, Z.X.1    Joklik, W.K.2
  • 23
    • 0021187586 scopus 로고
    • Extragenic suppression of temperature-sensitive phenotype in reovirus: Mapping suppressor mutations
    • McPhillips, T. H., and R. F. Ramig. 1984. Extragenic suppression of temperature-sensitive phenotype in reovirus: mapping suppressor mutations. Virology 135:428-439.
    • (1984) Virology , vol.135 , pp. 428-439
    • McPhillips, T.H.1    Ramig, R.F.2
  • 24
    • 0018836512 scopus 로고
    • Pyridoxal phosphate as a probe of reovirus transcriptase
    • Morgan, E. M., and D. W. Kingsbury. 1980. Pyridoxal phosphate as a probe of reovirus transcriptase. Biochemistry 19:484-489.
    • (1980) Biochemistry , vol.19 , pp. 484-489
    • Morgan, E.M.1    Kingsbury, D.W.2
  • 25
    • 0019425265 scopus 로고
    • Reovirus enzymes that modify messenger RNA are inhibition by perturbation of the lambda proteins
    • Morgan, E. M., and D. W. Kingsbury. 1981. Reovirus enzymes that modify messenger RNA are inhibition by perturbation of the lambda proteins. Virology 113:565-572.
    • (1981) Virology , vol.113 , pp. 565-572
    • Morgan, E.M.1    Kingsbury, D.W.2
  • 26
    • 0024401164 scopus 로고
    • A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses
    • Morozov, S. Y. 1989. A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses. Nucleic Acids Res. 17:5394.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5394
    • Morozov, S.Y.1
  • 27
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein μ1/μ1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration
    • Nibert, M. L., and B. N. Fields. 1992. A carboxy-terminal fragment of protein μ1/μ1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J. Virol. 66:6408-6418.
    • (1992) J. Virol. , vol.66 , pp. 6408-6418
    • Nibert, M.L.1    Fields, B.N.2
  • 28
    • 0010980518 scopus 로고
    • Early steps in reovirus infection of cells
    • E. Wimmer (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Nibert, M. L., and B. N. Fields. 1994. Early steps in reovirus infection of cells, p. 341-364. In E. Wimmer (ed.), Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 341-364
    • Nibert, M.L.1    Fields, B.N.2
  • 29
    • 0029834595 scopus 로고    scopus 로고
    • Non-random segregation of parental alleles in reovirus reassortants
    • Nibert, M. L., R. L. Margraf, and K. M. Coombs. 1996. Non-random segregation of parental alleles in reovirus reassortants. J. Virol. 70:7295-7300.
    • (1996) J. Virol. , vol.70 , pp. 7295-7300
    • Nibert, M.L.1    Margraf, R.L.2    Coombs, K.M.3
  • 30
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A., and N. Sonenberg. 1992. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11:2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 31
    • 0021153754 scopus 로고
    • Reovirus RNA transcriptase: Evidence for a conformational change during activation of the core particle
    • Powell, K. F., J. D. Harvey, and A. R. Bellamy. 1984. Reovirus RNA transcriptase: evidence for a conformational change during activation of the core particle. Virology 137:1-8.
    • (1984) Virology , vol.137 , pp. 1-8
    • Powell, K.F.1    Harvey, J.D.2    Bellamy, A.R.3
  • 32
    • 0024585746 scopus 로고
    • Studies on the mechanism of the antiviral activity of ribavirin against reovirus
    • Rankin, J. T., Jr., S. B. Eppes, J. B. Antczak, and W. K. Joklik. 1989. Studies on the mechanism of the antiviral activity of ribavirin against reovirus. Virology 168:147-158.
    • (1989) Virology , vol.168 , pp. 147-158
    • Rankin Jr., J.T.1    Eppes, S.B.2    Antczak, J.B.3    Joklik, W.K.4
  • 33
    • 0023673325 scopus 로고
    • Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3
    • Schiff, L. A., M. L. Nibert, M. S. Co, E. G. Brown, and B. N. Fields. 1988. Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3. Mol. Cell. Biol. 8:273-283.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 273-283
    • Schiff, L.A.1    Nibert, M.L.2    Co, M.S.3    Brown, E.G.4    Fields, B.N.5
  • 34
    • 0023646021 scopus 로고
    • Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase
    • Seliger, L. S., K. Zheng, and A. J. Shatkin. 1987. Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase. J. Biol. Chem. 262:16289-16293.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16289-16293
    • Seliger, L.S.1    Zheng, K.2    Shatkin, A.J.3
  • 35
    • 0017232972 scopus 로고
    • Reovirus mRNA: Transcription and translation
    • Shatkin, A. J., and G. W. Both. 1976. Reovirus mRNA: transcription and translation. Cell 7:305-313.
    • (1976) Cell , vol.7 , pp. 305-313
    • Shatkin, A.J.1    Both, G.W.2
  • 36
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus type 3
    • Smith, R. E., H. J. Zweerink, and W. K. Joklik. 1969. Polypeptide components of virions, top component and cores of reovirus type 3. Virology 39:791-810.
    • (1969) Virology , vol.39 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 37
    • 0027177215 scopus 로고
    • Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase
    • Starnes, M. C., and W. K. Joklik. 1993. Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase. Virology 193:356-366.
    • (1993) Virology , vol.193 , pp. 356-366
    • Starnes, M.C.1    Joklik, W.K.2
  • 38
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R. M., and T. A. Steitz. 1992. Structure of the recA protein-ADP complex. Nature 355:374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 39
    • 0027254336 scopus 로고
    • RNA-stimulated NTPase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus
    • Tamura, J. K., P. Warrener, and M. S. Collett. 1993. RNA-stimulated NTPase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus. Virology 193:1-10.
    • (1993) Virology , vol.193 , pp. 1-10
    • Tamura, J.K.1    Warrener, P.2    Collett, M.S.3
  • 40
    • 0001607723 scopus 로고
    • Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 41
    • 0017295002 scopus 로고
    • Studies on the structure of reovirus cores: Selective removal of polypeptide lambda 2
    • White, C. K., and H. J. Zweerink. 1976. Studies on the structure of reovirus cores: selective removal of polypeptide lambda 2. Virology 70:171-180.
    • (1976) Virology , vol.70 , pp. 171-180
    • White, C.K.1    Zweerink, H.J.2
  • 42
    • 0027432147 scopus 로고
    • Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2
    • Xu, P., S. E. Miller, and W. K. Joklik. 1993. Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2. Virology 197:726-731.
    • (1993) Virology , vol.197 , pp. 726-731
    • Xu, P.1    Miller, S.E.2    Joklik, W.K.3
  • 43
    • 0019798433 scopus 로고
    • Excess synthesis of viral mRNA 5′-terminal oligonucleotides by reovirus transcriptase
    • Yamakawa, M., Y. Furuichi, K. Nakashima, A. J. LaFiandra, and A. J. Shatkin. 1981. Excess synthesis of viral mRNA 5′-terminal oligonucleotides by reovirus transcriptase. J. Biol. Chem. 256:6507-6514.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6507-6514
    • Yamakawa, M.1    Furuichi, Y.2    Nakashima, K.3    LaFiandra, A.J.4    Shatkin, A.J.5
  • 44
    • 0020024958 scopus 로고
    • Reovirus transcriptase and capping enzymes are active in intact virions
    • Yamakawa, M., Y. Furuichi, and A. J. Shatkin. 1982. Reovirus transcriptase and capping enzymes are active in intact virions. Virology 118:157-168.
    • (1982) Virology , vol.118 , pp. 157-168
    • Yamakawa, M.1    Furuichi, Y.2    Shatkin, A.J.3
  • 45
    • 0030030595 scopus 로고    scopus 로고
    • The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles
    • Yin, P., M. Cheang, and K. M. Coombs. 1996. The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles. J. Virol. 70:1223-1227.
    • (1996) J. Virol. , vol.70 , pp. 1223-1227
    • Yin, P.1    Cheang, M.2    Coombs, K.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.