메뉴 건너뛰기




Volumn 44, Issue 18, 2005, Pages 6877-6888

Framework model for DNA polymerases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CRYSTAL STRUCTURE; DNA; MATHEMATICAL MODELS; STATISTICAL METHODS;

EID: 18244405770     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0477079     Document Type: Article
Times cited : (7)

References (30)
  • 2
    • 0037333239 scopus 로고    scopus 로고
    • Rotary Protein Motors
    • Oster, G., and Wang, H. Y. (2003) Rotary Protein Motors, Trends Cell Biol. 13, 114-121.
    • (2003) Trends Cell Biol. , vol.13 , pp. 114-121
    • Oster, G.1    Wang, H.Y.2
  • 3
    • 0034111877 scopus 로고    scopus 로고
    • The Mechanochemistry of Molecular Motors
    • Keller, D., and Bustamante, C. (2000) The Mechanochemistry of Molecular Motors, Biophys. J. 78, 541-556.
    • (2000) Biophys. J. , vol.78 , pp. 541-556
    • Keller, D.1    Bustamante, C.2
  • 4
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å 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 Å 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
  • 5
    • 0033578332 scopus 로고    scopus 로고
    • Structure-based Design of Taq DNA Polymerase with Improved Properties of Dideoxynucleotide Incorporation
    • Li, Y., Mitaxov, V., and Waksman, G. (1999) Structure-based Design of Taq DNA Polymerase with Improved Properties of Dideoxynucleotide Incorporation, Proc. Natl. Acad. Sci. U.S.A. 96, 9491-9496.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9491-9496
    • Li, Y.1    Mitaxov, V.2    Waksman, G.3
  • 6
    • 0028983795 scopus 로고
    • Crystal structure of Thermits aquaticus DNA polymerase
    • Kim, Y., Eom, S. H., Wang, J., Lee, D. S., Suh, S. W., and Steitz, T. A. (1995) Crystal structure of Thermits aquaticus DNA polymerase, Nature 376, 612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.S.4    Suh, S.W.5    Steitz, T.A.6
  • 7
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer, J. R., Mao, C., Braman, J. C., and Beese, L. S. (1998) Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal, Nature 391, 304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 8
    • 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., Vereine, 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    Vereine, G.L.3    Harrison, S.C.4
  • 9
    • 0033621167 scopus 로고    scopus 로고
    • Lamivudine (3TC) Resistance in HIV-1 reverse transcriptase involves steric hindrance with β-branched amino acids
    • Sarafianos, S. G., Das, K., Clark, A. D., Jr., Ding, J., Boyer, P. L., Hughes, S. H., and Arnold, E. (1999) Lamivudine (3TC) Resistance in HIV-1 reverse transcriptase involves steric hindrance with β-branched amino acids, Proc. Natl. Acad. Sci. U.S.A. 96, 10027-10032.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10027-10032
    • Sarafianos, S.G.1    Das, K.2    Clark Jr., A.D.3    Ding, J.4    Boyer, P.L.5    Hughes, S.H.6    Arnold, E.7
  • 11
    • 0032509101 scopus 로고    scopus 로고
    • Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double stranded DNA template primer and an antibody fAb fragment at 2.8 Å resolution
    • Ding, J., Das, K., Hsiou, Y., Sarafianos, S. G., Clark, A. D., Jr., Jacobo-Molina, A., Tantillo, C., Hughes, S. H., and Arnold, E. (1998) Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double stranded DNA template primer and an antibody fAb fragment at 2.8 Å resolution, J. Mol. Biol. 284, 1095-1111.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1095-1111
    • Ding, J.1    Das, K.2    Hsiou, Y.3    Sarafianos, S.G.4    Clark Jr., A.D.5    Jacobo-Molina, A.6    Tantillo, C.7    Hughes, S.H.8    Arnold, E.9
  • 12
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin, M. C., Wang, J., and Steitz, T. A. (2001) Structure of the replicating complex of a pol α family DNA polymerase, Cell 105, 657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 13
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya, M. R., Prasad, R., Wilson, S. H., Kraut, J., and Pelletier, H. (1997) Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism, Biochemistry 36, 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 15
    • 0027220197 scopus 로고
    • Conformational Coupling in DNA Polymerase Fidelity
    • Johnson, K. A. (1993) Conformational Coupling in DNA Polymerase Fidelity, Annu. Rev. Biochem. 62, 685-713.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 16
    • 0027365750 scopus 로고
    • Kinetic Mechanism of the DNA-dependent DNA Polymerase Activity of Human Immunodeficiency Virus Reverse Transcriptase
    • Hseih, J.-C., Zinnen, S., and Modrich, P. (1993) Kinetic Mechanism of the DNA-dependent DNA Polymerase Activity of Human Immunodeficiency Virus Reverse Transcriptase, J. Biol. Chem. 268, 24607-24613.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24607-24613
    • Hseih, J.-C.1    Zinnen, S.2    Modrich, P.3
  • 17
    • 0030918969 scopus 로고    scopus 로고
    • Analysis of Nucleotide Insertion and Extension at 8-Oxo-7,8- dihydroguanine by Replicative T7 Polymerase exo- and Human Immunodeficiency Virus-1 Reverse Transcriptase Using Steady-State and Pre-Steady-State Kinetics
    • Furge, L. L., and Guengerich, F. P. (1997) Analysis of Nucleotide Insertion and Extension at 8-Oxo-7,8-dihydroguanine by Replicative T7 Polymerase exo- and Human Immunodeficiency Virus-1 Reverse Transcriptase Using Steady-State and Pre-Steady-State Kinetics, Biochemistry 36, 6475-6487.
    • (1997) Biochemistry , vol.36 , pp. 6475-6487
    • Furge, L.L.1    Guengerich, F.P.2
  • 18
    • 0037154082 scopus 로고    scopus 로고
    • Effect of the O6 Substituent on Misincorporation Kinetics Catalyzed by DNA Polymerases at O6-Methylguanine and O6-Benzylguanine
    • Woodside, A. M., and Guengerich, F. P. (2002) Effect of the O6 Substituent on Misincorporation Kinetics Catalyzed by DNA Polymerases at O6-Methylguanine and O6-Benzylguanine, Biochemistry 41, 1027-1038.
    • (2002) Biochemistry , vol.41 , pp. 1027-1038
    • Woodside, A.M.1    Guengerich, F.P.2
  • 19
    • 0037154103 scopus 로고    scopus 로고
    • Misincorporation and Stalling at O6-Methylguanine and O6-Benzylguanine: Evidence for Inactive Polymerase Complexes
    • Woodside, A. M., and Guengerich, F. P. (2002) Misincorporation and Stalling at O6-Methylguanine and O6-Benzylguanine: Evidence for Inactive Polymerase Complexes, Biochemistry 41, 1039-1050.
    • (2002) Biochemistry , vol.41 , pp. 1039-1050
    • Woodside, A.M.1    Guengerich, F.P.2
  • 20
    • 0029883809 scopus 로고    scopus 로고
    • Kinetic Analysis of Pausing and Fidelity of Human Immunodeficiency Virus Type 1 Reverse Transcription
    • Pop, M. P., and Biebricher, C. K. (1996) Kinetic Analysis of Pausing and Fidelity of Human Immunodeficiency Virus Type 1 Reverse Transcription, Biochemistry 35, 5054-5062.
    • (1996) Biochemistry , vol.35 , pp. 5054-5062
    • Pop, M.P.1    Biebricher, C.K.2
  • 21
    • 0027092323 scopus 로고
    • Mechanism and Fidelity of HIV Reverse Transcriptase
    • Kati, W. M., Johnson, K. A., Jerva, L. F., and Anderson, K. S. (1992) Mechanism and Fidelity of HIV Reverse Transcriptase, J. Biol. Chem. 267, 25988-25997.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25988-25997
    • Kati, W.M.1    Johnson, K.A.2    Jerva, L.F.3    Anderson, K.S.4
  • 22
    • 0034594940 scopus 로고    scopus 로고
    • Single-Molecule Studies of the Effect of Template Tension on T7 DNA Polymerase Activity
    • Wuite, G. J. L., Smith, S. B., Young, M., Keller, D., and Bustamante, C. (2000) Single-Molecule Studies of the Effect of Template Tension on T7 DNA Polymerase Activity, Nature 404, 103-106.
    • (2000) Nature , vol.404 , pp. 103-106
    • Wuite, G.J.L.1    Smith, S.B.2    Young, M.3    Keller, D.4    Bustamante, C.5
  • 23
    • 0343811737 scopus 로고    scopus 로고
    • Single-Step Kinetics of HIV-1 Reverse Transcriptase Mutants Responsible for Virus Resistance to Nucleoside Inhibitors Zidovudine and 3-TC
    • Krebs, R., Immendorfer, U., Thrall, S. H., Wohrl, B. M., and Goody, R. S. (1997) Single-Step Kinetics of HIV-1 Reverse Transcriptase Mutants Responsible for Virus Resistance to Nucleoside Inhibitors Zidovudine and 3-TC, Biochemistry 36, 10292-10300.
    • (1997) Biochemistry , vol.36 , pp. 10292-10300
    • Krebs, R.1    Immendorfer, U.2    Thrall, S.H.3    Wohrl, B.M.4    Goody, R.S.5
  • 24
    • 0030703245 scopus 로고    scopus 로고
    • Pre-Steady-State Kinetic Characterization of Wild-Type and 3′-Azido-3′-deoxythymidine (AZT) Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Implication of RNA Directed DNA Polymerization in the Mechanism of AZT Resistance
    • Kerr, S. G., and Anderson, K. S. (1997) Pre-Steady-State Kinetic Characterization of Wild-Type and 3′-Azido-3′-deoxythymidine (AZT) Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Implication of RNA Directed DNA Polymerization in the Mechanism of AZT Resistance, Biochemistry 36, 14064-14070.
    • (1997) Biochemistry , vol.36 , pp. 14064-14070
    • Kerr, S.G.1    Anderson, K.S.2
  • 25
    • 0038143190 scopus 로고    scopus 로고
    • Dioxolane Guanosine 5′-Triphosphate, an Alternative Substrate Inhibitor of Wild-type and Mutant HTV-1 Reverse Transcriptase
    • Jeffrey, J. L., Feng, J. Y., Qi, C. C. R., Anderson, K. S., and Furman, P. A. (2003) Dioxolane Guanosine 5′-Triphosphate, an Alternative Substrate Inhibitor of Wild-type and Mutant HTV-1 Reverse Transcriptase, J. Biol. Chem. 278, 18971-18979.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18971-18979
    • Jeffrey, J.L.1    Feng, J.Y.2    Qi, C.C.R.3    Anderson, K.S.4    Furman, P.A.5
  • 26
    • 0030859022 scopus 로고    scopus 로고
    • Kinetic Analysis of Four HIV-1 Reverse Transcriptase Enzymes Mutated in the Primer Grip Region of p66
    • Wohrl, B. M., Krebs, R., Thralli, S. H., Le Grice, S. F. J., Scheidig, A. J., and Goody, R. S. (1997) Kinetic Analysis of Four HIV-1 Reverse Transcriptase Enzymes Mutated in the Primer Grip Region of p66, J. Biol. Chem. 272, 17581-17587.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17581-17587
    • Wohrl, B.M.1    Krebs, R.2    Thralli, S.H.3    Le Grice, S.F.J.4    Scheidig, A.J.5    Goody, R.S.6
  • 27
    • 0028033532 scopus 로고
    • Misincorporation and Mispaired Primer Extension by Human Immunodeficiency Virus Reverse Transcriptase
    • Zinnen, S., Hsieh, J.-C., and Modrich, P. (1994) Misincorporation and Mispaired Primer Extension by Human Immunodeficiency Virus Reverse Transcriptase, J. Biol. Chem. 269, 24195-24202.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24195-24202
    • Zinnen, S.1    Hsieh, J.-C.2    Modrich, P.3
  • 28
    • 0029670612 scopus 로고    scopus 로고
    • HIV-1 Reverse Transcriptase Resistance to Nonnucleoside Inhibitors
    • Spence, R. A., Anderson, K. S., and Johnson, K. A. (1996) HIV-1 Reverse Transcriptase Resistance to Nonnucleoside Inhibitors, Biochemistry 35, 1054-1063.
    • (1996) Biochemistry , vol.35 , pp. 1054-1063
    • Spence, R.A.1    Anderson, K.S.2    Johnson, K.A.3
  • 29
    • 0036829992 scopus 로고    scopus 로고
    • The Molecular Mechanism of Multidrug Resistance by the Q151M Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Its Suppression Using Boranophosphate Nucleotide Analogues
    • Deval, J., Selmi, B., Boretto, J., Egloff, M. P., Guerreiro, C., Sarfati, S., and Canard, B. (2002) The Molecular Mechanism of Multidrug Resistance by the Q151M Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Its Suppression Using Boranophosphate Nucleotide Analogues, J. Biol. Chem. 277, 42097-42104.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42097-42104
    • Deval, J.1    Selmi, B.2    Boretto, J.3    Egloff, M.P.4    Guerreiro, C.5    Sarfati, S.6    Canard, B.7
  • 30
    • 11144227942 scopus 로고    scopus 로고
    • Closing of the Fingers Domain Generates Motor Forces in the HIV Reverse Transcriptase
    • Lu, H., Macosko, J., Habel-Rodriquez, D., Keller, R. W., Brozik, J. A., and Keller, D. J. (2004) Closing of the Fingers Domain Generates Motor Forces in the HIV Reverse Transcriptase, J. Biol. Chem. 279, 54529-54532.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54529-54532
    • Lu, H.1    Macosko, J.2    Habel-Rodriquez, D.3    Keller, R.W.4    Brozik, J.A.5    Keller, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.