메뉴 건너뛰기




Volumn 41, Issue 1, 2013, Pages 253-263

DNA expansions generated by human Polμ on iterative sequences

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; DNA DIRECTED DNA POLYMERASE ALPHA; DNA DIRECTED DNA POLYMERASE BETA; DNA POLYMERASE; DNA POLYMERASE LAMBDA; DNA POLYMERASE MU; HISTIDINE; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84871769302     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1054     Document Type: Article
Times cited : (4)

References (57)
  • 1
    • 0035961198 scopus 로고    scopus 로고
    • DNA repair mechanisms
    • discussion 22-13
    • Hoeijmakers, J.H. (2001) DNA repair mechanisms. Maturitas, 38, 17-22, discussion 22-13.
    • (2001) Maturitas , vol.38 , pp. 17-22
    • Hoeijmakers, J.H.1
  • 6
    • 0037379215 scopus 로고    scopus 로고
    • Polymerase mu is a DNA-directed DNA/RNA polymerase
    • Nick McElhinny, S.A. and Ramsden, D.A. (2003) Polymerase mu is a DNA-directed DNA/RNA polymerase. Mol. Cell. Biol., 23, 2309-2315.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2309-2315
    • Nick McElhinny, S.A.1    Ramsden, D.A.2
  • 8
    • 7444228703 scopus 로고    scopus 로고
    • Overexpression of human DNA polymerase mu (Pol mu) in a Burkitt's lymphoma cell line affects the somatic hypermutation rate
    • Ruiz, J.F., Lucas, D., Garcia-Palomero, E., Saez, A.I., Gonzalez, M.A., Piris, M.A., Bernad, A. and Blanco, L. (2004) Overexpression of human DNA polymerase mu (Pol mu) in a Burkitt's lymphoma cell line affects the somatic hypermutation rate. Nucleic Acids Res., 32, 5861-5873.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5861-5873
    • Ruiz, J.F.1    Lucas, D.2    Garcia-Palomero, E.3    Saez, A.I.4    Gonzalez, M.A.5    Piris, M.A.6    Bernad, A.7    Blanco, L.8
  • 9
    • 0035158355 scopus 로고    scopus 로고
    • Highly frequent frameshift DNA synthesis by human DNA polymerase mu
    • Zhang, Y., Wu, X., Yuan, F., Xie, Z. and Wang, Z. (2001) Highly frequent frameshift DNA synthesis by human DNA polymerase mu. Mol. Cell. Biol., 21, 7995-8006.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7995-8006
    • Zhang, Y.1    Wu, X.2    Yuan, F.3    Xie, Z.4    Wang, Z.5
  • 10
    • 70349499328 scopus 로고    scopus 로고
    • Limited terminal transferase in human DNA polymerase mu defines the required balance between accuracy and efficiency in NHEJ
    • Andrade, P., Martin, M.J., Juarez, R., Lopez de Saro, F. and Blanco, L. (2009) Limited terminal transferase in human DNA polymerase mu defines the required balance between accuracy and efficiency in NHEJ. Proc. Natl Acad. Sci. USA, 106, 16203-16208.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16203-16208
    • Andrade, P.1    Martin, M.J.2    Juarez, R.3    Lopez De Saro, F.4    Blanco, L.5
  • 11
    • 44349155971 scopus 로고    scopus 로고
    • End-bridging is required for pol mu to efficiently promote repair of noncomplementary ends by nonhomologous end joining
    • Davis, B.J., Havener, J.M. and Ramsden, D.A. (2008) End-bridging is required for pol mu to efficiently promote repair of noncomplementary ends by nonhomologous end joining. Nucleic Acids Res., 36, 3085-3094.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3085-3094
    • Davis, B.J.1    Havener, J.M.2    Ramsden, D.A.3
  • 12
    • 0036567155 scopus 로고    scopus 로고
    • Human DNA polymerase mu (Pol mu) exhibits an unusual replication slippage ability at AAF lesion
    • Duvauchelle, J.B., Blanco, L., Fuchs, R.P. and Cordonnier, A.M. (2002) Human DNA polymerase mu (Pol mu) exhibits an unusual replication slippage ability at AAF lesion. Nucleic Acids Res., 30, 2061-2067.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2061-2067
    • Duvauchelle, J.B.1    Blanco, L.2    Fuchs, R.P.3    Cordonnier, A.M.4
  • 13
    • 34547135486 scopus 로고    scopus 로고
    • Involvement of DNA polymerase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells
    • Capp, J.P., Boudsocq, F., Besnard, A.G., Lopez, B.S., Cazaux, C., Hoffmann, J.S. and Canitrot, Y. (2007) Involvement of DNA polymerase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells. Nucleic Acids Res., 35, 3551-3560.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3551-3560
    • Capp, J.P.1    Boudsocq, F.2    Besnard, A.G.3    Lopez, B.S.4    Cazaux, C.5    Hoffmann, J.S.6    Canitrot, Y.7
  • 14
    • 0036293744 scopus 로고    scopus 로고
    • Association of DNA polymerase mu (pol mu) with Ku and ligase IV: Role for pol mu in end-joining double-strand break repair
    • Mahajan, K.N., Nick McElhinny, S.A., Mitchell, B.S. and Ramsden, D.A. (2002) Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair. Mol. Cell. Biol., 22, 5194-5202.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5194-5202
    • Mahajan, K.N.1    Nick McElhinny, S.A.2    Mitchell, B.S.3    Ramsden, D.A.4
  • 16
    • 33745997776 scopus 로고    scopus 로고
    • Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in vivo
    • Bertocci, B., De Smet, A., Weill, J.C. and Reynaud, C.A. (2006) Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in vivo. Immunity, 25, 31-41.
    • (2006) Immunity , vol.25 , pp. 31-41
    • Bertocci, B.1    De Smet, A.2    Weill, J.C.3    Reynaud, C.A.4
  • 17
    • 78049376599 scopus 로고    scopus 로고
    • Lack of DNA polymerase mu affects the kinetics of DNA double-strand break repair and impacts on cellular senescence
    • Chayot, R., Danckaert, A., Montagne, B. and Ricchetti, M. (2010) Lack of DNA polymerase mu affects the kinetics of DNA double-strand break repair and impacts on cellular senescence. DNA Repair (Amst), 9, 1187-1199.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 1187-1199
    • Chayot, R.1    Danckaert, A.2    Montagne, B.3    Ricchetti, M.4
  • 18
    • 84855339814 scopus 로고    scopus 로고
    • DNA polymerase mu is a global player in the repair of non-homologous end-joining substrates
    • Chayot, R., Montagne, B. and Ricchetti, M. (2012) DNA polymerase mu is a global player in the repair of non-homologous end-joining substrates. DNA Repair (Amst), 11, 22-34.
    • (2012) DNA Repair (Amst) , vol.11 , pp. 22-34
    • Chayot, R.1    Montagne, B.2    Ricchetti, M.3
  • 21
    • 0141483284 scopus 로고    scopus 로고
    • The frameshift infidelity of human DNA polymerase lambda. Implications for function
    • Bebenek, K., Garcia-Diaz, M., Blanco, L. and Kunkel, T.A. (2003) The frameshift infidelity of human DNA polymerase lambda. Implications for function. J. Biol. Chem., 278, 34685-34690.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34685-34690
    • Bebenek, K.1    Garcia-Diaz, M.2    Blanco, L.3    Kunkel, T.A.4
  • 22
    • 0021872030 scopus 로고
    • The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations
    • Kunkel, T.A. (1985) The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations. J. Biol. Chem., 260, 5787-5796.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5787-5796
    • Kunkel, T.A.1
  • 23
    • 0347723976 scopus 로고    scopus 로고
    • Lesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity
    • Covo, S., Blanco, L. and Livneh, Z. (2004) Lesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity. J. Biol. Chem., 279, 859-865.
    • (2004) J. Biol. Chem. , vol.279 , pp. 859-865
    • Covo, S.1    Blanco, L.2    Livneh, Z.3
  • 24
    • 0035201633 scopus 로고    scopus 로고
    • The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders
    • Bowater, R.P. and Wells, R.D. (2001) The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders. Prog. Nucleic Acid Res. Mol. Biol., 66, 159-202.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 159-202
    • Bowater, R.P.1    Wells, R.D.2
  • 25
    • 22244446185 scopus 로고    scopus 로고
    • Advances in mechanisms of genetic instability related to hereditary neurological diseases
    • Wells, R.D., Dere, R., Hebert, M.L., Napierala, M. and Son, L.S. (2005) Advances in mechanisms of genetic instability related to hereditary neurological diseases. Nucleic Acids Res., 33, 3785-3798.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3785-3798
    • Wells, R.D.1    Dere, R.2    Hebert, M.L.3    Napierala, M.4    Son, L.S.5
  • 26
    • 26944440117 scopus 로고    scopus 로고
    • Toward a unified theory for repeat expansions
    • Mirkin, S.M. (2005) Toward a unified theory for repeat expansions. Nat. Struct. Mol. Biol., 12, 635-637.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 635-637
    • Mirkin, S.M.1
  • 27
    • 34250878426 scopus 로고    scopus 로고
    • Expandable DNA repeats and human disease
    • Mirkin, S.M. (2007) Expandable DNA repeats and human disease. Nature, 447, 932-940.
    • (2007) Nature , vol.447 , pp. 932-940
    • Mirkin, S.M.1
  • 28
  • 29
    • 0032708840 scopus 로고    scopus 로고
    • Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice
    • Manley, K., Shirley, T.L., Flaherty, L. and Messer, A. (1999) Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice. Nat. Genet., 23, 471-473.
    • (1999) Nat. Genet. , vol.23 , pp. 471-473
    • Manley, K.1    Shirley, T.L.2    Flaherty, L.3    Messer, A.4
  • 30
    • 0037081784 scopus 로고    scopus 로고
    • Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins
    • van den Broek, W.J., Nelen, M.R., Wansink, D.G., Coerwinkel, M.M., te Riele, H., Groenen, P.J. and Wieringa, B. (2002) Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins. Hum. Mol. Genet., 11, 191-198.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 191-198
    • Van Den Broek, W.J.1    Nelen, M.R.2    Wansink, D.G.3    Coerwinkel, M.M.4    Te Riele, H.5    Groenen, P.J.6    Wieringa, B.7
  • 31
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • Bogdanov, M.B., Andreassen, O.A., Dedeoglu, A., Ferrante, R.J. and Beal, M.F. (2001) Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease. J. Neurochem., 79, 1246-1249.
    • (2001) J. Neurochem. , vol.79 , pp. 1246-1249
    • Bogdanov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 32
    • 34249337762 scopus 로고    scopus 로고
    • OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells
    • Kovtun, I.V., Liu, Y., Bjoras, M., Klungland, A., Wilson, S.H. and McMurray, C.T. (2007) OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells. Nature, 447, 447-452.
    • (2007) Nature , vol.447 , pp. 447-452
    • Kovtun, I.V.1    Liu, Y.2    Bjoras, M.3    Klungland, A.4    Wilson, S.H.5    McMurray, C.T.6
  • 37
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta 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 beta 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
  • 38
    • 84871192960 scopus 로고    scopus 로고
    • DNA-binding determinants promoting NHEJ by human Polm
    • Martin, M.J., Juarez, R. and Blanco, L. (2012) DNA-binding determinants promoting NHEJ by human Polm. Nucleic Acids Res., 40, 11389-11403.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11389-11403
    • Martin, M.J.1    Juarez, R.2    Blanco, L.3
  • 39
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase beta is processive
    • Singhal, R.K. and Wilson, S.H. (1993) Short gap-filling synthesis by DNA polymerase beta is processive. J. Biol. Chem., 268, 15906-15911.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 40
    • 0013997442 scopus 로고
    • Frameshift mutations and the genetic code. This paper is dedicated to Professor Theodosius Dobzhansky on the occasion of his 66th birthday
    • Streisinger, G., Okada, Y., Emrich, J., Newton, J., Tsugita, A., Terzaghi, E. and Inouye, M. (1966) Frameshift mutations and the genetic code. This paper is dedicated to Professor Theodosius Dobzhansky on the occasion of his 66th birthday. Cold Spring Harb. Symp. Quant. Biol., 31, 77-84.
    • (1966) Cold Spring Harb. Symp. Quant. Biol. , vol.31 , pp. 77-84
    • Streisinger, G.1    Okada, Y.2    Emrich, J.3    Newton, J.4    Tsugita, A.5    Terzaghi, E.6    Inouye, M.7
  • 41
    • 33750041949 scopus 로고    scopus 로고
    • A specific loop in human DNA polymerase mu allows switching between creative and DNA-instructed synthesis
    • Juarez, R., Ruiz, J.F., Nick McElhinny, S.A., Ramsden, D. and Blanco, L. (2006) A specific loop in human DNA polymerase mu allows switching between creative and DNA-instructed synthesis. Nucleic Acids Res., 34, 4572-4582.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4572-4582
    • Juarez, R.1    Ruiz, J.F.2    Nick McElhinny, S.A.3    Ramsden, D.4    Blanco, L.5
  • 43
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel, T.A. (2004) DNA replication fidelity. J. Biol. Chem., 279, 16895-16898.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 44
    • 0025309892 scopus 로고
    • Frameshift errors initiated by nucleotide misincorporation
    • Bebenek, K. and Kunkel, T.A. (1990) Frameshift errors initiated by nucleotide misincorporation. Proc. Natl Acad. Sci. USA, 87, 4946-4950.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4946-4950
    • Bebenek, K.1    Kunkel, T.A.2
  • 45
    • 0023790391 scopus 로고
    • Mutagenesis by transient misalignment
    • Kunkel, T.A. and Soni, A. (1988) Mutagenesis by transient misalignment. J. Biol. Chem., 263, 14784-14789.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14784-14789
    • Kunkel, T.A.1    Soni, A.2
  • 46
    • 0030836866 scopus 로고    scopus 로고
    • Fidelity of Escherichia coli DNA polymerase III holoenzyme. the effects of beta, gamma complex processivity proteins and epsilon proofreading exonuclease on nucleotide misincorporation efficiencies
    • Bloom, L.B., Chen, X., Fygenson, D.K., Turner, J., O'Donnell, M. and Goodman, M.F. (1997) Fidelity of Escherichia coli DNA polymerase III holoenzyme. The effects of beta, gamma complex processivity proteins and epsilon proofreading exonuclease on nucleotide misincorporation efficiencies. J. Biol. Chem., 272, 27919-27930.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27919-27930
    • Bloom, L.B.1    Chen, X.2    Fygenson, D.K.3    Turner, J.4    O'Donnell, M.5    Goodman, M.F.6
  • 47
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase beta violates the "a-rule". Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts
    • Efrati, E., Tocco, G., Eritja, R., Wilson, S.H. and Goodman, M.F. (1997) Abasic translesion synthesis by DNA polymerase beta violates the "A-rule". Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts. J. Biol. Chem., 272, 2559-2569.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 48
    • 69049118173 scopus 로고    scopus 로고
    • Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region
    • Romain, F., Barbosa, I., Gouge, J., Rougeon, F. and Delarue, M. (2009) Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region. Nucleic Acids Res., 37, 4642-4656.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4642-4656
    • Romain, F.1    Barbosa, I.2    Gouge, J.3    Rougeon, F.4    Delarue, M.5
  • 49
    • 0033137336 scopus 로고    scopus 로고
    • Effects of temperature, Mg2+ concentration and mismatches on triplet-repeat expansion during DNA replication in vitro
    • Lyons-Darden, T. and Topal, M.D. (1999) Effects of temperature, Mg2+ concentration and mismatches on triplet-repeat expansion during DNA replication in vitro. Nucleic Acids Res., 27, 2235-2240.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2235-2240
    • Lyons-Darden, T.1    Topal, M.D.2
  • 50
    • 0032570797 scopus 로고    scopus 로고
    • Analysis of strand slippage in DNA polymerase expansions of CAG/CTG triplet repeats associated with neurodegenerative disease
    • Petruska, J., Hartenstine, M.J. and Goodman, M.F. (1998) Analysis of strand slippage in DNA polymerase expansions of CAG/CTG triplet repeats associated with neurodegenerative disease. J. Biol. Chem., 273, 5204-5210.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5204-5210
    • Petruska, J.1    Hartenstine, M.J.2    Goodman, M.F.3
  • 51
    • 0033600752 scopus 로고    scopus 로고
    • Replication slippage of different DNA polymerases is inversely related to their strand displacement efficiency
    • Canceill, D., Viguera, E. and Ehrlich, S.D. (1999) Replication slippage of different DNA polymerases is inversely related to their strand displacement efficiency. J. Biol. Chem., 274, 27481-27490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27481-27490
    • Canceill, D.1    Viguera, E.2    Ehrlich, S.D.3
  • 52
    • 0027014233 scopus 로고
    • DNA structure, mutations, and human genetic disease
    • Sinden, R.R. and Wells, R.D. (1992) DNA structure, mutations, and human genetic disease. Curr. Opin. Biotechnol., 3, 612-622.
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 612-622
    • Sinden, R.R.1    Wells, R.D.2
  • 53
    • 0034613187 scopus 로고    scopus 로고
    • Dinucleotide repeat expansion catalyzed by bacteriophage T4 DNA polymerase in vitro
    • da Silva, E.F. and Reha-Krantz, L.J. (2000) Dinucleotide repeat expansion catalyzed by bacteriophage T4 DNA polymerase in vitro. J. Biol. Chem., 275, 31528-31535.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31528-31535
    • Da Silva, E.F.1    Reha-Krantz, L.J.2
  • 54
    • 0036828873 scopus 로고    scopus 로고
    • Weak strand displacement activity enables human DNA polymerase beta to expand CAG/CTG triplet repeats at strand breaks
    • Hartenstine, M.J., Goodman, M.F. and Petruska, J. (2002) Weak strand displacement activity enables human DNA polymerase beta to expand CAG/CTG triplet repeats at strand breaks. J. Biol. Chem., 277, 41379-41389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41379-41389
    • Hartenstine, M.J.1    Goodman, M.F.2    Petruska, J.3
  • 55
    • 0028277915 scopus 로고
    • Error-prone replication of repeated DNA sequences by T7 DNA polymerase in the absence of its processivity subunit
    • Kunkel, T.A., Patel, S.S. and Johnson, K.A. (1994) Error-prone replication of repeated DNA sequences by T7 DNA polymerase in the absence of its processivity subunit. Proc. Natl Acad. Sci. USA, 91, 6830-6834.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6830-6834
    • Kunkel, T.A.1    Patel, S.S.2    Johnson, K.A.3
  • 56
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman, E.R. (1992) Protein oxidation and aging. Science, 257, 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.