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Volumn 73, Issue 2, 1999, Pages 1302-1308

Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase of the DExH box family

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NUCLEOSIDE TRIPHOSPHATE; PHOSPHATASE; VIRUS ENZYME;

EID: 0032933848     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.2.1302-1308.1999     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 0023185989 scopus 로고
    • Identification of the vaccinia virus gene encoding nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase
    • Broyles, S. S., and B. Moss. 1987. Identification of the vaccinia virus gene encoding nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase. J. Virol. 61:1738-1742.
    • (1987) J. Virol. , vol.61 , pp. 1738-1742
    • Broyles, S.S.1    Moss, B.2
  • 2
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype 1b hepatitis C virus: A feasible mechanism of unwinding duplex RNA
    • Cho, H.-S., N.-C. Ha, L.-W. Kang, K. M. Chung, S. H. Back, S. K. Jang, and B.-H. Oh. 1998. Crystal structure of RNA helicase from genotype 1b hepatitis C virus: a feasible mechanism of unwinding duplex RNA. J. Biol. Chem. 273:15045-15052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15045-15052
    • Cho, H.-S.1    Ha, N.-C.2    Kang, L.-W.3    Chung, K.M.4    Back, S.H.5    Jang, S.K.6    Oh, B.-H.7
  • 3
    • 0032486254 scopus 로고    scopus 로고
    • Vaccinia virus nucleoside triphosphate phosphohydrolase I is an essential viral early gene transcription termination factor
    • Christen, L. M., M. Sanders, C. Wiler, and E. G. Niles. 1998. Vaccinia virus nucleoside triphosphate phosphohydrolase I is an essential viral early gene transcription termination factor. Virology 245:360-371.
    • (1998) Virology , vol.245 , pp. 360-371
    • Christen, L.M.1    Sanders, M.2    Wiler, C.3    Niles, E.G.4
  • 4
    • 0029825580 scopus 로고    scopus 로고
    • An ATPase component of the transcription elongation complex is required for factor-dependent transcription termination by vaccinia RNA polymerase
    • Deng, L., and S. Shuman. 1996. An ATPase component of the transcription elongation complex is required for factor-dependent transcription termination by vaccinia RNA polymerase. J. Biol. Chem. 271:29386-29392.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29386-29392
    • Deng, L.1    Shuman, S.2
  • 5
    • 0032519829 scopus 로고    scopus 로고
    • Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination
    • Deng, L., and S. Shuman. 1998. Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination. Genes Dev. 12:538-546.
    • (1998) Genes Dev. , vol.12 , pp. 538-546
    • Deng, L.1    Shuman, S.2
  • 6
    • 0028047403 scopus 로고
    • A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II
    • George, J. W., R. M. Brosh, and S. W. Matson. 1994. A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. J. Mol. Biol. 235:424-435.
    • (1994) J. Mol. Biol. , vol.235 , pp. 424-435
    • George, J.W.1    Brosh, R.M.2    Matson, S.W.3
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0030050636 scopus 로고    scopus 로고
    • The ORxGRxGRxxxG 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 ORxGRxGRxxxG 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
  • 10
    • 0029917572 scopus 로고    scopus 로고
    • Vaccinia virus RNA helicase: Nucleic acid specificity in duplex unwinding
    • Gross, C. H., and S. Shuman. 1996. Vaccinia virus RNA helicase: nucleic acid specificity in duplex unwinding. J. Virol. 70:2615-2619.
    • (1996) J. Virol. , vol.70 , pp. 2615-2619
    • Gross, C.H.1    Shuman, S.2
  • 11
    • 0031901334 scopus 로고    scopus 로고
    • The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication
    • Gross, C. H., and S. Shuman. 1998. The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication. J. Virol. 72:4729-4736.
    • (1998) J. Virol. , vol.72 , pp. 4729-4736
    • Gross, C.H.1    Shuman, S.2
  • 12
    • 0030741828 scopus 로고    scopus 로고
    • A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein
    • Heilek, G. M., and M. G. Peterson. 1997. A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein. J. Virol. 71:6264-6266.
    • (1997) J. Virol. , vol.71 , pp. 6264-6266
    • Heilek, G.M.1    Peterson, M.G.2
  • 13
    • 0027178594 scopus 로고
    • Transcriptional activator components and poxvirus DNA-dependent ATPases comprise a single family
    • Henikoff, S. 1993. Transcriptional activator components and poxvirus DNA-dependent ATPases comprise a single family. Trends Biochem. Sci. 18:291-292.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 291-292
    • Henikoff, S.1
  • 14
    • 0031800746 scopus 로고    scopus 로고
    • Mutational analysis of the yeast DEAH-box splicing factor Prp16
    • Hotz, H. R, and B. Schwer. 1998. Mutational analysis of the yeast DEAH-box splicing factor Prp16. Genetics 149:807-815.
    • (1998) Genetics , vol.149 , pp. 807-815
    • Hotz, H.R.1    Schwer, B.2
  • 15
    • 0013627747 scopus 로고    scopus 로고
    • Mutational analysis of the hepatitis C virus RNA helicase
    • Kim, D. W., J. Kim, Y. Gwack, J. H. Han, and J. Choe. 1997. Mutational analysis of the hepatitis C virus RNA helicase. J. Virol. 71:9400-9409.
    • (1997) J. Virol. , vol.71 , pp. 9400-9409
    • Kim, D.W.1    Kim, J.2    Gwack, Y.3    Han, J.H.4    Choe, J.5
  • 16
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J. L., K. A. Morgenstern, J. P. Griffith, M. D. Dwyer, J. A. Thomson, M. A. Murcko, C. Lim, and P. R. Caron. 1998. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6:89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lim, C.7    Caron, P.R.8
  • 17
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by crystal structure of complexes of E. coli rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., J. Hsieh, G. H. Gauss, T. M. Lohman, and G. Waksman. 1997. Major domain swiveling revealed by crystal structure of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90:635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 19
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of gtp hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 20
    • 0016204488 scopus 로고
    • Two nucleic acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus. Nucleotide substrate and polynucleotide cofactor specificities
    • Paoletti, E., and B. Moss. 1974. Two nucleic acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus. Nucleotide substrate and polynucleotide cofactor specificities. J. Biol. Chem. 249:3281-3286.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3281-3286
    • Paoletti, E.1    Moss, B.2
  • 21
    • 0016236771 scopus 로고
    • Two nucleic acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus: Purification and characterization
    • Paoletti, E., H. Rosemond-Hornbeak, and B. Moss. 1974. Two nucleic acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus: purification and characterization. J. Biol. Chem. 249:3273-3280.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3273-3280
    • Paoletti, E.1    Rosemond-Hornbeak, H.2    Moss, B.3
  • 22
    • 0027494565 scopus 로고
    • The HR1GRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause, A., N. Méthot, and N. Sonenberg. 1993. The HR1GRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol. Cell. Biol. 13:6789-6798.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6789-6798
    • Pause, A.1    Méthot, N.2    Sonenberg, N.3
  • 23
    • 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
  • 24
    • 0030986934 scopus 로고    scopus 로고
    • SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions
    • Pazin, M. J., and J. T. Kadonaga. 1997. SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions. Cell 88:737-740.
    • (1997) Cell , vol.88 , pp. 737-740
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 25
    • 0011100726 scopus 로고
    • Molecular cloning, encoding sequence, and expression of vaccinia nucleic acid-dependent nucleoside triphosphatase gene
    • Rodriguez, J. F., J. S. Kahn, and M. Esteban. 1986. Molecular cloning, encoding sequence, and expression of vaccinia nucleic acid-dependent nucleoside triphosphatase gene. Proc. Natl. Acad. Sci. USA 83:9566-9570.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9566-9570
    • Rodriguez, J.F.1    Kahn, J.S.2    Esteban, M.3
  • 26
    • 0026490908 scopus 로고
    • Vaccinia virus RNA helicase: An essential enzyme related to the DE-H family of RNA-dependent NTPases
    • Shuman, S. 1992. Vaccinia virus RNA helicase: an essential enzyme related to the DE-H family of RNA-dependent NTPases. Proc. Natl. Acad. Sci. USA 89:10935-10939.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10935-10939
    • Shuman, S.1
  • 27
    • 0027241018 scopus 로고
    • Vaccinia virus RNA helicase: Directionality and substrate specificity
    • Shuman, S. 1993. Vaccinia virus RNA helicase: directionality and substrate specificity. J. Biol. Chem. 268:11798-11802.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11798-11802
    • Shuman, S.1
  • 28
    • 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
  • 30
    • 0024095589 scopus 로고
    • Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP
    • Sung, P., D. Higgins, L. Prakash, and S. Prakash. 1988. Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP. EMBO J. 7:3263-3269.
    • (1988) EMBO J. , vol.7 , pp. 3263-3269
    • Sung, P.1    Higgins, D.2    Prakash, L.3    Prakash, S.4
  • 32
    • 0026726616 scopus 로고
    • ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes
    • Zavitz, K. H., and K. J. Marians. 1992. ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes. J. Biol. Chem. 267:6933-6940.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6933-6940
    • Zavitz, K.H.1    Marians, K.J.2


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