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Volumn 43, Issue 18, 2004, Pages 5149-5158

Poliovirus RNA-Dependent RNA Polymerase (3Dpol): Kinetic, Thermodynamic, and Structural Analysis of Ribonucleotide Selection

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; RNA; THERMODYNAMICS;

EID: 2442461170     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035429s     Document Type: Article
Times cited : (64)

References (31)
  • 4
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J. L., Long, A. M., and Schultz, S. C. (1997) Structure of the RNA-dependent RNA polymerase of poliovirus, Structure 5, 1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 5
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H., Chopra, R., Verdine, G. L., and Harrison, S. C. (1998) Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance, Science 282, 1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 7
    • 0034090927 scopus 로고    scopus 로고
    • pol): Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub)
    • pol): Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub), J. Biol. Chem. 275, 5329-5336.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5329-5336
    • Arnold, J.J.1    Cameron, C.E.2
  • 8
    • 0026026192 scopus 로고
    • An induced-fit kinetic mechanism for DNA replication fidelity: Direct measurement by single-turnover kinetics
    • Wong, I., Patel, S. S., and Johnson, K. A. (1991) An induced-fit kinetic mechanism for DNA replication fidelity: direct measurement by single-turnover kinetics, Biochemistry 30, 526-537
    • (1991) Biochemistry , vol.30 , pp. 526-537
    • Wong, I.1    Patel, S.S.2    Johnson, K.A.3
  • 9
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • Patel, S. S., Wong, I., and Johnson, K. A. (1991) Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant, Biochemistry 30, 511-525.
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 10
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano, L., Horovitz, A., Avron, B., Bycroft, M., and Fersht, A. R. (1990) Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles, Biochemistry 29, 9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 11
    • 0023657031 scopus 로고
    • Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
    • Fersht, A. R. (1987) Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis, Biochemistry 26, 8031-8307.
    • (1987) Biochemistry , vol.26 , pp. 8031-8307
    • Fersht, A.R.1
  • 12
    • 0026681635 scopus 로고
    • Quantitative interpretations of double mutations of enzymes
    • Mildvan, A. S., Weber, D. J., and Kuliopulos, A. (1992) Quantitative interpretations of double mutations of enzymes, Arch. Biochem. Biophys. 294, 327-340.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 327-340
    • Mildvan, A.S.1    Weber, D.J.2    Kuliopulos, A.3
  • 14
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg, C. A., Cable, M. B., Ferrari, E., Hong, Z., Mannarino, A. F., and Weber, P. C. (1999) Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site, Nat. Struct. Biol. 6, 937-943.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 16
    • 0037059758 scopus 로고    scopus 로고
    • Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase
    • Ng, K. K., Cherney, M. M., Vazquez, A. L., Machin, A., Alonso, J. M., Parra, F., and James, M. N. (2002) Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase, J. Biol. Chem. 277, 1381-1387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1381-1387
    • Ng, K.K.1    Cherney, M.M.2    Vazquez, A.L.3    Machin, A.4    Alonso, J.M.5    Parra, F.6    James, M.N.7
  • 17
  • 18
    • 0025743809 scopus 로고
    • The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses
    • Koonin, E. V. (1991) The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses, J. Gen. Virol. 72, 2197-2206.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2197-2206
    • Koonin, E.V.1
  • 19
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • Johnson, S. J., Taylor, J. S., and Beese L. S. (2003) Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations, Proc. Natl. Acad. Sci. U.S.A. 100, 3895-3900.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 20
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin, Y. W., and Steitz, T. A. (2002) Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase, Science 298, 1387-1395.
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 21
    • 0033579380 scopus 로고    scopus 로고
    • Structure of a transcribing T7 RNA polymerase initiation complex
    • Cheetham, G. M., and Steitz, T. A. (1999) Structure of a transcribing T7 RNA polymerase initiation complex, Science 286, 2305-2309.
    • (1999) Science , vol.286 , pp. 2305-2309
    • Cheetham, G.M.1    Steitz, T.A.2
  • 22
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublie, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2. 2 A resolution, Nature 391, 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 23
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese, L. S., Derbyshire, V., and Steitz, T. A. (1993) Structure of DNA polymerase I Klenow fragment bound to duplex DNA, Science 260, 352-355.
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 24
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li, Y., Korolev, S., and Waksman, G. (1998) Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation, EMBO J. 17, 7514-7525.
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 25
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with DNA: Implications for catalytic mechanism, processivity, and fidelity
    • Pelletier, H., Sawaya, M. R., Wolfle, W., Wilson, S. H., and Kraut J. (1996) Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity, Biochemistry 35, 12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 26
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
    • Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., and Kraut, J. (1994) Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP, Science 264, 1891-18903.
    • (1994) Science , vol.264 , pp. 1891-18903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 28
    • 0030854581 scopus 로고    scopus 로고
    • Mechanism of ribose 2′-group discrimination by an RNA polymerase
    • Huang, Y., Eckstein, F., Padilla, R., and Sousa R. (1997) Mechanism of ribose 2′-group discrimination by an RNA polymerase, Biochemistry 36, 8231-8242.
    • (1997) Biochemistry , vol.36 , pp. 8231-8242
    • Huang, Y.1    Eckstein, F.2    Padilla, R.3    Sousa, R.4
  • 29
    • 0037183526 scopus 로고    scopus 로고
    • A reexamination of the nucleotide incorporation fidelity of DNA polymerases
    • Showalter, A. K., and Tsai, M.-D. (2002) A reexamination of the nucleotide incorporation fidelity of DNA polymerases, Biochemistry 41, 10571-10576.
    • (2002) Biochemistry , vol.41 , pp. 10571-10576
    • Showalter, A.K.1    Tsai, M.-D.2
  • 30
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69
    • Wang, J., Sattar, A. K., Wang, C. C., Karam, J. D., Konigsberg, W. H., and Steitz, T. A. (1997) Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69, Cell 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 31
    • 0032584219 scopus 로고    scopus 로고
    • A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides
    • Astatke, M., Ng, K., Grindley, N. D., and Joyce, C. M. (1998) A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides, Proc. Natl. Acad. Sci. U.S.A. 95, 3402-3407.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3402-3407
    • Astatke, M.1    Ng, K.2    Grindley, N.D.3    Joyce, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.