메뉴 건너뛰기




Volumn 6, Issue 10, 2010, Pages 774-781

Genome instability due to ribonucleotide incorporation into DNA

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA POLYMERASE; GENOMIC DNA; GLYCINE; LEUCINE; METHIONINE; RIBONUCLEOTIDE; DNA DIRECTED DNA POLYMERASE; FUNGAL DNA; RIBONUCLEASE H; RIBONUCLEASE HII;

EID: 77956921247     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.424     Document Type: Article
Times cited : (328)

References (37)
  • 1
    • 0031042722 scopus 로고    scopus 로고
    • Choosing the right sugar: How polymerases select a nucleotide substrate
    • Joyce, C.M. Choosing the right sugar: how polymerases select a nucleotide substrate. Proc. Natl. Acad. Sci. USA 94, 1619-1622 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1619-1622
    • Joyce, C.M.1
  • 2
    • 77950406088 scopus 로고    scopus 로고
    • Abundant ribonucleotide incorporation into DNA by yeast replicative polymerases
    • Nick McElhinny, S.A., et al. Abundant ribonucleotide incorporation into DNA by yeast replicative polymerases. Proc. Natl. Acad. Sci. USA 107, 4949-4954 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 4949-4954
    • Nick McElhinny, S.A.1
  • 4
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T.W. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140, 1-22 (1994).
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 5
    • 34447336941 scopus 로고    scopus 로고
    • Yeast DNA polymerase epsilon participates in leading-strand DNA replication
    • Pursell, Z.F., Isoz, I., Lundstrom, E.B., Johansson, E. & Kunkel, T.A. Yeast DNA polymerase epsilon participates in leading-strand DNA replication. Science 317, 127-130 (2007).
    • (2007) Science , vol.317 , pp. 127-130
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.B.3    Johansson, E.4    Kunkel, T.A.5
  • 7
    • 33644633822 scopus 로고    scopus 로고
    • Lagging strand replication proteins in genome stability and DNA repair
    • Rossi, M.L., Purohit, V., Brandt, P.D. & Bambara, R.A. Lagging strand replication proteins in genome stability and DNA repair. Chem. Rev. 106, 453-473 (2006).
    • (2006) Chem. Rev. , vol.106 , pp. 453-473
    • Rossi, M.L.1    Purohit, V.2    Brandt, P.D.3    Bambara, R.A.4
  • 8
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers, P.M. Polymerase dynamics at the eukaryotic DNA replication fork. J. Biol. Chem. 284, 4041-4045 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4041-4045
    • Burgers, P.M.1
  • 9
    • 0242317682 scopus 로고    scopus 로고
    • An error-prone family y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses ásteric gate residue for discrimination against ribonucleotides
    • DeLucia, A.M., Grindley, N.D. & Joyce, C.M. An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses ásteric gate residue for discrimination against ribonucleotides. Nucleic Acids Res. 31, 4129-4137 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4129-4137
    • Delucia, A.M.1    Grindley, N.D.2    Joyce, C.M.3
  • 10
    • 0345188651 scopus 로고    scopus 로고
    • A single tyrosine prevents insertion of ribonucleotides in the eukaryotic-type phi29 DNA polymerase
    • Bonnin, A., Lazaro, J.M., Blanco, L. & Salas, M. A single tyrosine prevents insertion of ribonucleotides in the eukaryotic-type phi29 DNA polymerase. J. Mol. Biol. 290, 241-251 (1999).
    • (1999) J. Mol. Biol. , vol.290 , pp. 241-251
    • Bonnin, A.1    Lazaro, J.M.2    Blanco, L.3    Salas, M.4
  • 11
    • 0033564079 scopus 로고    scopus 로고
    • Determinants of nucleotide sugar recognition in an archaeon DNA polymerase
    • Gardner, A.F. & Jack, W.E. Determinants of nucleotide sugar recognition in an archaeon DNA polymerase. Nucleic Acids Res. 27, 2545-2553 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2545-2553
    • Gardner, A.F.1    Jack, W.E.2
  • 12
    • 0037072265 scopus 로고    scopus 로고
    • A conserved Tyr residue is required for sugar selectivity in a Pol alpha DNA polymerase
    • Yang, G., Franklin, M., Li, J., Lin, T.C. & Konigsberg, W. A conserved Tyr residue is required for sugar selectivity in a Pol alpha DNA polymerase. Biochemistry 41, 10256-10261 (2002).
    • (2002) Biochemistry , vol.41 , pp. 10256-10261
    • Yang, G.1    Franklin, M.2    Li, J.3    Lin, T.C.4    Konigsberg, W.5
  • 13
    • 0034805293 scopus 로고    scopus 로고
    • In vivo consequences of putative active site mutations in yeast DNA polymerases alpha, epsilon, delta, and zeta
    • Pavlov, Y.I., Shcherbakova, P.V. & Kunkel, T.A. In vivo consequences of putative active site mutations in yeast DNA polymerases alpha, epsilon, delta, and zeta. Genetics 159, 47-64 (2001).
    • (2001) Genetics , vol.159 , pp. 47-64
    • Pavlov, Y.I.1    Shcherbakova, P.V.2    Kunkel, T.A.3
  • 14
    • 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. & Joyce, C.M. A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides. Proc. Natl. Acad. Sci. USA 95, 3402-3407 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3402-3407
    • Astatke, M.1    Ng, K.2    Grindley, N.D.3    Joyce, C.M.4
  • 15
    • 0035374671 scopus 로고    scopus 로고
    • The conserved active site motif A of Escherichia coli DNA polymerase i is highly mutable
    • Shinkai, A., Patel, P.H. & Loeb, L.A. The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutable. J. Biol. Chem. 276, 18836-18842 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18836-18842
    • Shinkai, A.1    Patel, P.H.2    Loeb, L.A.3
  • 16
    • 0037168516 scopus 로고    scopus 로고
    • Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts
    • Rydberg, B. & Game, J. Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts. Proc. Natl. Acad. Sci. USA 99, 16654-16659 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16654-16659
    • Rydberg, B.1    Game, J.2
  • 17
    • 0025911370 scopus 로고
    • Ribonuclease H from K562 human erythroleukemia cells. Purification, characterization, and substrate specificity
    • Eder, P.S. & Walder, J.A. Ribonuclease H from K562 human erythroleukemia cells. Purification, characterization, and substrate specificity. J. Biol. Chem. 266, 6472-6479 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 6472-6479
    • Eder, P.S.1    Walder, J.A.2
  • 18
    • 0027213005 scopus 로고
    • Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA
    • Eder, P.S., Walder, R.Y. & Walder, J.A. Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA. Biochimie 75, 123-126 (1993).
    • (1993) Biochimie , vol.75 , pp. 123-126
    • Eder, P.S.1    Walder, R.Y.2    Walder, J.A.3
  • 19
    • 61349102407 scopus 로고    scopus 로고
    • Ribonuclease H: The enzymes in eukaryotes
    • Cerritelli, S.M. & Crouch, R.J. Ribonuclease H: the enzymes in eukaryotes. FEBS J. 276, 1494-1505 (2009).
    • (2009) FEBS J. , vol.276 , pp. 1494-1505
    • Cerritelli, S.M.1    Crouch, R.J.2
  • 20
    • 34250642401 scopus 로고    scopus 로고
    • Regulation of B family DNA polymerase fidelity by a conserved active site residue: Characterization of M644W, M644L and M644F mutants of yeast DNA polymerase epsilon
    • Pursell, Z.F., Isoz, I., Lundstrom, E.B., Johansson, E. & Kunkel, T.A. Regulation of B family DNA polymerase fidelity by a conserved active site residue: characterization of M644W, M644L and M644F mutants of yeast DNA polymerase epsilon. Nucleic Acids Res. 35, 3076-3086 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3076-3086
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.B.3    Johansson, E.4    Kunkel, T.A.5
  • 21
    • 0037423223 scopus 로고    scopus 로고
    • Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by relaxed feedback inhibition of ribonucleotide reductase
    • Chabes, A., et al. Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by relaxed feedback inhibition of ribonucleotide reductase. Cell 112, 391-401 (2003).
    • (2003) Cell , vol.112 , pp. 391-401
    • Chabes, A.1
  • 22
    • 0033512305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease
    • Qiu, J., Qian, Y., Frank, P., Wintersberger, U. & Shen, B. Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol. Cell. Biol. 19, 8361-8371 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8361-8371
    • Qiu, J.1    Qian, Y.2    Frank, P.3    Wintersberger, U.4    Shen, B.5
  • 23
    • 0034666029 scopus 로고    scopus 로고
    • Mutational spectrum analysis of RNase H(35) deficient Saccharomyces cerevisiae using fluorescence-based directed termination PCR
    • Chen, J.Z., Qiu, J., Shen, B. & Holmquist, G.P. Mutational spectrum analysis of RNase H(35) deficient Saccharomyces cerevisiae using fluorescence-based directed termination PCR. Nucleic Acids Res. 28, 3649-3656 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3649-3656
    • Chen, J.Z.1    Qiu, J.2    Shen, B.3    Holmquist, G.P.4
  • 25
    • 0032947675 scopus 로고    scopus 로고
    • Purification of Saccharomyces cerevisiae RNase H(70) and identification of the corresponding gene
    • Frank, P., Braunshofer-Reiter, C., Karwan, A., Grimm, R. & Wintersberger, U. Purification of Saccharomyces cerevisiae RNase H(70) and identification of the corresponding gene. FEBS Lett. 450, 251-256 (1999).
    • (1999) FEBS Lett. , vol.450 , pp. 251-256
    • Frank, P.1    Braunshofer-Reiter, C.2    Karwan, A.3    Grimm, R.4    Wintersberger, U.5
  • 26
    • 0025309892 scopus 로고
    • Frameshift errors initiated by nucleotide misincorporation
    • Bebenek, K. & Kunkel, T.A. Frameshift errors initiated by nucleotide misincorporation. Proc. Natl. Acad. Sci. USA 87, 4946-4950 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4946-4950
    • Bebenek, K.1    Kunkel, T.A.2
  • 27
    • 0024429338 scopus 로고
    • Fidelity of DNA polymerase i and the DNA polymerase I-DNA primase complex from Saccharomyces cerevisiae
    • Kunkel, T.A., Hamatake, R.K., Motto-Fox, J., Fitzgerald, M.P. & Sugino, A. Fidelity of DNA polymerase I and the DNA polymerase I-DNA primase complex from Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 4447-4458 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4447-4458
    • Kunkel, T.A.1    Hamatake, R.K.2    Motto-Fox, J.3    Fitzgerald, M.P.4    Sugino, A.5
  • 28
    • 0029017879 scopus 로고
    • Purification and properties of wild-type and exonuclease-deficient DNA polymerase II from Escherichia coli
    • Cai, H., Yu, H., McEntee, K., Kunkel, T.A. & Goodman, M.F. Purification and properties of wild-type and exonuclease-deficient DNA polymerase II from Escherichia coli. J. Biol. Chem. 270, 15327-15335 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 15327-15335
    • Cai, H.1    Yu, H.2    McEntee, K.3    Kunkel, T.A.4    Goodman, M.F.5
  • 29
    • 33746522835 scopus 로고    scopus 로고
    • Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection
    • Crow, Y.J., et al. Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat. Genet. 38, 910-916 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 910-916
    • Crow, Y.J.1
  • 30
    • 0025228710 scopus 로고
    • Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme
    • Hamatake, R.K., et al. Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. J. Biol. Chem. 265, 4072-4083 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 4072-4083
    • Hamatake, R.K.1
  • 31
    • 0037515466 scopus 로고    scopus 로고
    • The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae
    • Chilkova, O., Jonsson, B.H. & Johansson, E. The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae. J. Biol. Chem. 278, 14082-14086 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14082-14086
    • Chilkova, O.1    Jonsson, B.H.2    Johansson, E.3
  • 32
    • 0347379857 scopus 로고    scopus 로고
    • The efficiency and specificity of apurinic/apyrimidinic site bypass by human DNA polymerase ? and Sulfolobus solfataricus Dpo4
    • Kokoska, R.J., McCulloch, S.D. & Kunkel, T.A. The efficiency and specificity of apurinic/apyrimidinic site bypass by human DNA polymerase ? and Sulfolobus solfataricus Dpo4. J. Biol. Chem. 278, 50537-50545 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50537-50545
    • Kokoska, R.J.1    McCulloch, S.D.2    Kunkel, T.A.3
  • 33
    • 0037162552 scopus 로고    scopus 로고
    • Correlation of somatic hypermutation specificity and A-T base pair substitution errors by DNA polymerase eta during copying of a mouse immunoglobulin kappa light chain transgene
    • Pavlov, Y.I., et al. Correlation of somatic hypermutation specificity and A-T base pair substitution errors by DNA polymerase eta during copying of a mouse immunoglobulin kappa light chain transgene. Proc. Natl. Acad. Sci. USA 99, 9954-9959 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9954-9959
    • Pavlov, Y.I.1
  • 34
    • 0033624527 scopus 로고    scopus 로고
    • DNA polymerase epsilon mutant that specifically causes +1 frameshift mutations within homonucleotide runs in yeast
    • Kirchner, J.M., Tran, H. & Resnick, M.A.A. DNA polymerase epsilon mutant that specifically causes +1 frameshift mutations within homonucleotide runs in yeast. Genetics 155, 1623-1632 (2000).
    • (2000) Genetics , vol.155 , pp. 1623-1632
    • Kirchner, J.M.1    Tran, H.2    Resnick, M.A.A.3
  • 36
    • 55249101776 scopus 로고    scopus 로고
    • Evidence for lesion bypass by yeast replicative DNA polymerases during DNA damage
    • Sabouri, N., Viberg, J., Goyal, D.K., Johansson, E. & Chabes, A. Evidence for lesion bypass by yeast replicative DNA polymerases during DNA damage. Nucleic Acids Res. 36, 5660-5667 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5660-5667
    • Sabouri, N.1    Viberg, J.2    Goyal, D.K.3    Johansson, E.4    Chabes, A.5
  • 37
    • 0032915375 scopus 로고    scopus 로고
    • Mutator phenotypes conferred by MLH1 overexpression and by heterozygosity for mlh1 mutations
    • Shcherbakova, P.V. & Kunkel, T.A. Mutator phenotypes conferred by MLH1 overexpression and by heterozygosity for mlh1 mutations. Mol. Cell. Biol. 19, 3177-3183 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3177-3183
    • Shcherbakova, P.V.1    Kunkel, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.