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Volumn 116, Issue 6, 2004, Pages 803-816

Structures of mismatch replication errors observed in a DNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; PRIMER DNA;

EID: 1642588255     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00252-1     Document Type: Article
Times cited : (265)

References (40)
  • 1
    • 0028902990 scopus 로고
    • Structure of an RNA double helix including uracil-uracil base pairs in an internal loop
    • Baeyens K.J., De Bondt H.L., Holbrook S.R. Structure of an RNA double helix including uracil-uracil base pairs in an internal loop. Nat. Struct. Biol. 2:1995;56-62.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 56-62
    • Baeyens, K.J.1    De Bondt, H.L.2    Holbrook, S.R.3
  • 2
    • 0027848722 scopus 로고
    • Multi-stage proofreading in DNA replication
    • Beckman R.A., Loeb L.A. Multi-stage proofreading in DNA replication. Q. Rev. Biophys. 26:1993;225-331.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 225-331
    • Beckman, R.A.1    Loeb, L.A.2
  • 3
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam C.A., Steitz T.A. Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8:1998;54-63.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 4
    • 0026029379 scopus 로고
    • A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
    • Carroll S.S., Cowart M., Benkovic S.J. A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity. Biochemistry. 30:1991;804-813.
    • (1991) Biochemistry , vol.30 , pp. 804-813
    • Carroll, S.S.1    Cowart, M.2    Benkovic, S.J.3
  • 5
    • 0028075950 scopus 로고
    • Proofreading DNA: Recognition of aberrant DNA termini by the Klenow Fragment of DNA polymerase I
    • Carver T.J., Hochstrasser R.A., Millar D.P. Proofreading DNA. recognition of aberrant DNA termini by the Klenow Fragment of DNA polymerase I Proc. Natl. Acad. Sci. USA. 91:1994;10670-10674.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10670-10674
    • Carver, T.J.1    Hochstrasser, R.A.2    Millar, D.P.3
  • 7
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublié S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 9
    • 0025783442 scopus 로고
    • Fidelity mechanisms in DNA replication
    • Echols H., Goodman M.F. Fidelity mechanisms in DNA replication. Annu. Rev. Biochem. 60:1991;477-511.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 477-511
    • Echols, H.1    Goodman, M.F.2
  • 10
    • 0025736013 scopus 로고
    • Mechanism of DNA replication fidelity for three mutants of DNA polymerase I: Klenow Fragment KF(exo+), KF(polA5), and KF(exo-)
    • Eger B.T., Kuchta R.D., Carroll S.S., Benkovic P.A., Dahlberg M.E., Joyce C.M., Benkovic S.J. Mechanism of DNA replication fidelity for three mutants of DNA polymerase I. Klenow Fragment KF(exo+), KF(polA5), and KF(exo-) Biochemistry. 30:1991;1441-1448.
    • (1991) Biochemistry , vol.30 , pp. 1441-1448
    • Eger, B.T.1    Kuchta, R.D.2    Carroll, S.S.3    Benkovic, P.A.4    Dahlberg, M.E.5    Joyce, C.M.6    Benkovic, S.J.7
  • 11
    • 0035812844 scopus 로고    scopus 로고
    • Error-prone DNA polymerases: Novel structures and the benefits of infidelity
    • Friedberg E.C., Fischhaber P.L., Kisker C. Error-prone DNA polymerases. novel structures and the benefits of infidelity Cell. 107:2001;9-12.
    • (2001) Cell , vol.107 , pp. 9-12
    • Friedberg, E.C.1    Fischhaber, P.L.2    Kisker, C.3
  • 13
    • 0026698636 scopus 로고
    • Extension of base mispairs by Taq DNA polymerase: Implications for single nucleotide discrimination in PCR
    • Huang M.M., Arnheim N., Goodman M.F. Extension of base mispairs by Taq DNA polymerase. implications for single nucleotide discrimination in PCR Nucleic Acids Res. 20:1992;4567-4573.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4567-4573
    • Huang, M.M.1    Arnheim, N.2    Goodman, M.F.3
  • 14
    • 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., Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase. implications for drug resistance Science. 282:1998;1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 15
    • 0022505062 scopus 로고
    • Structure of an adenine.cytosine base pair in DNA and its implications for mismatch repair
    • Hunter W.N., Brown T., Anand N.N., Kennard O. Structure of an adenine.cytosine base pair in DNA and its implications for mismatch repair. Nature. 320:1986;552-555.
    • (1986) Nature , vol.320 , pp. 552-555
    • Hunter, W.N.1    Brown, T.2    Anand, N.N.3    Kennard, O.4
  • 17
    • 0027318776 scopus 로고
    • Crystal structure of Human Immunodeficiency Virus Type I reverse transcriptase complexed with double-stranded DNA at 3.0 Å shows bent DNA
    • Jacobo-Molina A., Arnold E. Crystal structure of Human Immunodeficiency Virus Type I reverse transcriptase complexed with double-stranded DNA at 3.0 Å shows bent DNA. Proc. Natl. Acad. Sci. USA. 90:1993;6320-6324.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6320-6324
    • Jacobo-Molina, A.1    Arnold, E.2
  • 18
    • 0027220197 scopus 로고
    • Conformational coupling in DNA polymerase fidelity
    • Johnson K.A. Conformational coupling in DNA polymerase fidelity. Annu. Rev. Biochem. 62:1993;685-713.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 685-713
    • Johnson, K.A.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., Beese L.S. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc. Natl. Acad. Sci. USA. 100:2003;3895-3900.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 20
    • 0024395470 scopus 로고
    • How DNA travels between the separate polymerase and 3′-5′ exonuclease sites of DNA polymerase I (Klenow Fragment)
    • Joyce C.M. How DNA travels between the separate polymerase and 3′-5′ exonuclease sites of DNA polymerase I (Klenow Fragment). J. Biol. Chem. 264:1989;10858-10866.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10858-10866
    • Joyce, C.M.1
  • 21
    • 0028206048 scopus 로고
    • Function and structure relationships in DNA polymerases
    • Joyce C.M., Steitz T.A. Function and structure relationships in DNA polymerases. Annu. Rev. Biochem. 63:1994;777-822.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 777-822
    • Joyce, C.M.1    Steitz, T.A.2
  • 22
    • 0026483792 scopus 로고
    • Reactions at the polymerase active site that contribute to the fidelity of Escherichia coli DNA polymerase I (Klenow Fragment)
    • Joyce C.M., Sun X.C., Grindley N.D.F. Reactions at the polymerase active site that contribute to the fidelity of Escherichia coli DNA polymerase I (Klenow Fragment). J. Biol. Chem. 267:1992;24485-24500.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24485-24500
    • Joyce, C.M.1    Sun, X.C.2    Grindley, N.D.F.3
  • 23
    • 0024819551 scopus 로고
    • Oligonucleotide structure: A decade of results from single crystal X- ray diffraction studies
    • Kennard O., Hunter W.N. Oligonucleotide structure. a decade of results from single crystal X- ray diffraction studies Q. Rev. Biophys. 22:1989;327-379.
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 327-379
    • Kennard, O.1    Hunter, W.N.2
  • 25
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391:1998;304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 26
    • 0023770718 scopus 로고
    • Kinetic mechanism whereby DNA polymerase I (Klenow) replicates DNA with high fidelity
    • Kuchta R.D., Benkovic P., Benkovic S.J. Kinetic mechanism whereby DNA polymerase I (Klenow) replicates DNA with high fidelity. Biochemistry. 27:1988;6716-6725.
    • (1988) Biochemistry , vol.27 , pp. 6716-6725
    • Kuchta, R.D.1    Benkovic, P.2    Benkovic, S.J.3
  • 28
    • 0035019856 scopus 로고    scopus 로고
    • Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP- trapped ternary complex of Klentaq1: Insights into nucleotide incorporation and selectivity
    • Li Y., Waksman G. Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP- trapped ternary complex of Klentaq1. insights into nucleotide incorporation and selectivity Protein Sci. 10:2001;1225-1233.
    • (2001) Protein Sci. , vol.10 , pp. 1225-1233
    • Li, Y.1    Waksman, G.2
  • 29
    • 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., Waksman G. 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. 17:1998;7514-7525.
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 30
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H., Boudsocq F., Woodgate R., Yang W. Crystal structure of a Y-family DNA polymerase in action. a mechanism for error-prone and lesion-bypass replication Cell. 107:2001;91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 31
    • 0034698001 scopus 로고    scopus 로고
    • A-form conformational motifs in ligand-bound DNA structures
    • Lu X.J., Shakked Z., Olson W.K. A-form conformational motifs in ligand-bound DNA structures. J. Mol. Biol. 300:2000;819-840.
    • (2000) J. Mol. Biol. , vol.300 , pp. 819-840
    • Lu, X.J.1    Shakked, Z.2    Olson, W.K.3
  • 32
    • 0030693128 scopus 로고    scopus 로고
    • Kinetics of DNA polymerase I (Klenow fragment exo-) activity on damaged DNA templates: Effect of proximal and distal template damage on DNA synthesis
    • Miller H., Grollman A.P. Kinetics of DNA polymerase I (Klenow fragment exo-) activity on damaged DNA templates. effect of proximal and distal template damage on DNA synthesis Biochemistry. 36:1997;15336-15342.
    • (1997) Biochemistry , vol.36 , pp. 15336-15342
    • Miller, H.1    Grollman, A.P.2
  • 33
    • 0024962334 scopus 로고
    • Recognition and binding of template-primers containing defined abasic sites by Drosophila DNA polymerase alpha holoenzyme
    • Ng L., Weiss S.J., Fisher P.A. Recognition and binding of template-primers containing defined abasic sites by Drosophila DNA polymerase alpha holoenzyme. J. Biol. Chem. 264:1989;13018-13023.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13018-13023
    • Ng, L.1    Weiss, S.J.2    Fisher, P.A.3
  • 35
    • 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., Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP. Science. 264:1994;1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 36
    • 0024670547 scopus 로고
    • Proofreading by the epsilon subunit of Escherichia coli DNA polymerase III increases the fidelity of calf thymus DNA polymerase alpha
    • Perrino F.W., Loeb L.A. Proofreading by the epsilon subunit of Escherichia coli DNA polymerase III increases the fidelity of calf thymus DNA polymerase alpha. Proc. Natl. Acad. Sci. USA. 86:1989;3085-3088.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3085-3088
    • Perrino, F.W.1    Loeb, L.A.2
  • 37
    • 0027475856 scopus 로고
    • Crystal structure of an oligonucleotide duplex containing G.G base pairs: Influence of mispairing on DNA backbone conformation
    • Skelly J.V., Edwards K.J., Jenkins T.C., Neidle S. Crystal structure of an oligonucleotide duplex containing G.G base pairs. influence of mispairing on DNA backbone conformation Proc. Natl. Acad. Sci. USA. 90:1993;804-808.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 804-808
    • Skelly, J.V.1    Edwards, K.J.2    Jenkins, T.C.3    Neidle, S.4
  • 38
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz T.A. DNA polymerases. structural diversity and common mechanisms J. Biol. Chem. 274:1999;17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 39
    • 0026702250 scopus 로고
    • Interaction of Drosophila DNA polymerase alpha holoenzyme with synthetic template-primers containing mismatched primer bases or propanodeoxyguanosine adducts at various positions in template and primer regions
    • Weiss S.J., Fisher P.A. Interaction of Drosophila DNA polymerase alpha holoenzyme with synthetic template-primers containing mismatched primer bases or propanodeoxyguanosine adducts at various positions in template and primer regions. J. Biol. Chem. 267:1992;18520-18526.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18520-18526
    • Weiss, S.J.1    Fisher, P.A.2
  • 40
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science. 298:2002;1387-1395.
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2


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