메뉴 건너뛰기




Volumn 200, Issue , 2004, Pages 156-164

Sibling rivalry: Competition between Pol X family members in V(D)J recombination and general double strand break repair

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE; DNA POLYMERASE; LYMPHOCYTE ANTIGEN RECEPTOR; RNA POLYMERASE;

EID: 3242876769     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0105-2896.2004.00160.x     Document Type: Review
Times cited : (51)

References (78)
  • 1
    • 0032518680 scopus 로고    scopus 로고
    • Ku protein stimulates DNA end joining by mammalian DNA ligases: A direct role for Ku in repair of DNA double-strand breaks
    • Ramsden DA, Gellert M. Ku protein stimulates DNA end joining by mammalian DNA ligases: a direct role for Ku in repair of DNA double-strand breaks. EMBO J 1998;17:609-614.
    • (1998) EMBO J , vol.17 , pp. 609-614
    • Ramsden, D.A.1    Gellert, M.2
  • 2
    • 0037124373 scopus 로고    scopus 로고
    • Synapsis of DNA ends by DNA-dependent protein kinase
    • DeFazio LG, Stansel RM, Griffith JD, Chu G. Synapsis of DNA ends by DNA-dependent protein kinase. EMBO J 2002;21:3192-3200.
    • (2002) EMBO J , vol.21 , pp. 3192-3200
    • DeFazio, L.G.1    Stansel, R.M.2    Griffith, J.D.3    Chu, G.4
  • 4
    • 0034714199 scopus 로고    scopus 로고
    • Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase
    • Chen L, Trujillo K, Sung P, Tomkinson AE. Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem 2000;275:26196-26205.
    • (2000) J Biol Chem , vol.275 , pp. 26196-26205
    • Chen, L.1    Trujillo, K.2    Sung, P.3    Tomkinson, A.E.4
  • 5
    • 0037423743 scopus 로고    scopus 로고
    • Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment
    • Calsou P, Delteil C, Frit P, Drouet J, Salles B. Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. J Mol Biol 2003;326:93-103.
    • (2003) J Mol Biol , vol.326 , pp. 93-103
    • Calsou, P.1    Delteil, C.2    Frit, P.3    Drouet, J.4    Salles, B.5
  • 6
    • 0035968210 scopus 로고    scopus 로고
    • Accurate in vitro end joining of a DNA double strand break with partially cohesive 3′-overhangs and 3′-phosphoglycolate termini: Effect of Ku on repair fidelity
    • Chen S, et al. Accurate in vitro end joining of a DNA double strand break with partially cohesive 3′-overhangs and 3′-phosphoglycolate termini: effect of Ku on repair fidelity. J Biol Chem 2001;276:24323-24330.
    • (2001) J Biol Chem , vol.276 , pp. 24323-24330
    • Chen, S.1
  • 7
    • 0034234487 scopus 로고    scopus 로고
    • DNA double-strand break repair in cell-free extracts from Ku80-deficient cells: Implications for Ku serving as an alignment factor in non-homologous DNA end joining
    • Feldmann E, Schmiemann V, Goedecke W, Reichenberger S, Pfeiffer P. DNA double-strand break repair in cell-free extracts from Ku80-deficient cells: implications for Ku serving as an alignment factor in non-homologous DNA end joining. Nucleic Acids Res 2000;28:2585-2596.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2585-2596
    • Feldmann, E.1    Schmiemann, V.2    Goedecke, W.3    Reichenberger, S.4    Pfeiffer, P.5
  • 9
    • 0028078579 scopus 로고
    • Mechanisms of overlap formation in nonhomologous DNA end joining
    • Pfeiffer P, Thode S, Hancke J, Vielmetter W. Mechanisms of overlap formation in nonhomologous DNA end joining. Mol Cell Biol 1994;14:888-895.
    • (1994) Mol Cell Biol , vol.14 , pp. 888-895
    • Pfeiffer, P.1    Thode, S.2    Hancke, J.3    Vielmetter, W.4
  • 10
    • 0022976432 scopus 로고
    • Nonhomologous recombination in mammalian cells: Role for short sequence homologies in the joining reaction
    • Roth DB, Wilson JH. Nonhomologous recombination in mammalian cells: role for short sequence homologies in the joining reaction. Mol Cell Biol 1986;6:4295-4304.
    • (1986) Mol Cell Biol , vol.6 , pp. 4295-4304
    • Roth, D.B.1    Wilson, J.H.2
  • 13
    • 0029414789 scopus 로고
    • Mice lacking terminal deoxynucleotidyl transferase: Adult mice with a fetal antigen receptor repertoire
    • Gilfillan S, Benoist C, Mathis D. Mice lacking terminal deoxynucleotidyl transferase: adult mice with a fetal antigen receptor repertoire. Immunol Rev 1995;148:201-219.
    • (1995) Immunol Rev , vol.148 , pp. 201-219
    • Gilfillan, S.1    Benoist, C.2    Mathis, D.3
  • 14
    • 0035941229 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases: Proposal for a revised nomenclature
    • Burgers PM, et al. Eukaryotic DNA polymerases: proposal for a revised nomenclature. J Biol Chem 2001;276:43487-43490.
    • (2001) J Biol Chem , vol.276 , pp. 43487-43490
    • Burgers, P.M.1
  • 16
    • 0033551662 scopus 로고    scopus 로고
    • Efficient processing of DNA ends during yeast nonhomologous end joining. Evidence for a DNA polymerase beta (Pol4)-dependent pathway
    • Wilson TE, Lieber MR. Efficient processing of DNA ends during yeast nonhomologous end joining. Evidence for a DNA polymerase beta (Pol4)-dependent pathway. J Biol Chem 1999;274:23599-23609.
    • (1999) J Biol Chem , vol.274 , pp. 23599-23609
    • Wilson, T.E.1    Lieber, M.R.2
  • 17
    • 0028845729 scopus 로고
    • Purification and enzymatic and functional characterization of DNA polymerase beta-like enzyme, POL4. expressed during yeast meiosis
    • Budd ME, Campbell JL. Purification and enzymatic and functional characterization of DNA polymerase beta-like enzyme, POL4. expressed during yeast meiosis. Methods Enzymol 1995;262:108-130.
    • (1995) Methods Enzymol , vol.262 , pp. 108-130
    • Budd, M.E.1    Campbell, J.L.2
  • 18
    • 0027937623 scopus 로고
    • The yeast Saccharomyces cerevisiae DNA polymerase IV: Possible involvement in double strand break DNA repair
    • Leem SH, Ropp PA, Sugino A. The yeast Saccharomyces cerevisiae DNA polymerase IV: possible involvement in double strand break DNA repair. Nucleic Acids Res 1994;22:3011-3017.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3011-3017
    • Leem, S.H.1    Ropp, P.A.2    Sugino, A.3
  • 19
    • 0028013486 scopus 로고
    • Two different types of double-strand breaks in Saccharomyces cerevisiae are repaired by similar RAD52-independent, nonhomologous recombination events
    • Kramer KM, Brock JA, Bloom K, Moore JK, Haber JE. Two different types of double-strand breaks in Saccharomyces cerevisiae are repaired by similar RAD52-independent, nonhomologous recombination events. Mol Cell Biol 1994;14:1293-1301.
    • (1994) Mol Cell Biol , vol.14 , pp. 1293-1301
    • Kramer, K.M.1    Brock, J.A.2    Bloom, K.3    Moore, J.K.4    Haber, J.E.5
  • 20
    • 0029976325 scopus 로고    scopus 로고
    • Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae
    • Moore JK, Haber JE. Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae. Mol Cell Biol 1996;16:2164-2173.
    • (1996) Mol Cell Biol , vol.16 , pp. 2164-2173
    • Moore, J.K.1    Haber, J.E.2
  • 21
    • 0242634246 scopus 로고    scopus 로고
    • DNA polymerase mu (Pol mu), homologous TdT, could act a DNA mutator eukaryotic cells
    • Dominguez O, et al. DNA polymerase mu (Pol mu), homologous TdT, could act a DNA mutator eukaryotic cells. EMBO J 2000;19:1731-1742.
    • (2000) EMBO J , vol.19 , pp. 1731-1742
    • Dominguez, O.1
  • 22
    • 0034666193 scopus 로고    scopus 로고
    • Two novel human and mouse DNA polymerases of the polX family
    • Aoufouchi S, et al. Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res 2000;28:3684-3693.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3684-3693
    • Aoufouchi, S.1
  • 23
    • 0030837472 scopus 로고    scopus 로고
    • V(D)J recombination in Ku86-deficient mice: Distinct effects on coding, signal, and hybrid joint formation
    • Bogue MA, Wang C, Zhu C, Roth DB. V(D)J recombination in Ku86-deficient mice: distinct effects on coding, signal, and hybrid joint formation. Immunity 1997;7:37-47.
    • (1997) Immunity , vol.7 , pp. 37-47
    • Bogue, M.A.1    Wang, C.2    Zhu, C.3    Roth, D.B.4
  • 24
    • 0035312286 scopus 로고    scopus 로고
    • Ku80 is required for addition of N nucleotides to V(D)J recombination junctions by terminal deoxynucleotidyl transferase
    • Purugganan MM, Shah S, Kearney JF, Roth DB. Ku80 is required for addition of N nucleotides to V(D)J recombination junctions by terminal deoxynucleotidyl transferase. Nucleic Acids Res 2001;29:1638-1646.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1638-1646
    • Purugganan, M.M.1    Shah, S.2    Kearney, J.F.3    Roth, D.B.4
  • 25
    • 0028283180 scopus 로고
    • Abnormal deletions in the T-cell receptor delta locus of mouse thymocytes
    • Fish SM, Bosma MJ. Abnormal deletions in the T-cell receptor delta locus of mouse thymocytes. Mol Cell Biol 1994;14:4455-4464.
    • (1994) Mol Cell Biol , vol.14 , pp. 4455-4464
    • Fish, S.M.1    Bosma, M.J.2
  • 26
    • 0033598831 scopus 로고    scopus 로고
    • Association of terminal deoxynucleotidyl transferase with Ku
    • Mahajan KN, et al. Association of terminal deoxynucleotidyl transferase with Ku. Proc Natl Acad Sci USA 1999;96:13926-13931.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13926-13931
    • Mahajan, K.N.1
  • 27
    • 0033565878 scopus 로고    scopus 로고
    • Modulation of terminal deoxynucleotidyltransferase activity by the DNA-dependent protein kinase
    • Mickelsen S, Snyder C, Trujillo K, Bogue M, Roth DB, Meek K. Modulation of terminal deoxynucleotidyltransferase activity by the DNA-dependent protein kinase. J Immunol 1999;163:834-843.
    • (1999) J Immunol , vol.163 , pp. 834-843
    • Mickelsen, S.1    Snyder, C.2    Trujillo, K.3    Bogue, M.4    Roth, D.B.5    Meek, K.6
  • 28
    • 0041931065 scopus 로고    scopus 로고
    • Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu
    • Bertocci B, De Smet A, Berek C, Weill JC, Reynaud CA. Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu. Immunity 2003;19:203-211.
    • (2003) Immunity , vol.19 , pp. 203-211
    • Bertocci, B.1    De Smet, A.2    Berek, C.3    Weill, J.C.4    Reynaud, C.A.5
  • 29
    • 0035158355 scopus 로고    scopus 로고
    • Highly frequent frameshift DNA synthesis by human DNA polymerase mu
    • Zhang Y, Wu X, Yuan F, Xie Z, Wang Z. Highly frequent frameshift DNA synthesis by human DNA polymerase mu. Mol Cell Biol 2001;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
  • 31
    • 0037379215 scopus 로고    scopus 로고
    • Polymerase mu is a DNA-directed DNA/RNA polymerase
    • Nick McElhinny SA, Ramsden DA. Polymerase mu is a DNA-directed DNA/RNA polymerase. Mol Cell Biol 2003;23: 2309-2315.
    • (2003) Mol Cell Biol , vol.23 , pp. 2309-2315
    • Nick McElhinny, S.A.1    Ramsden, D.A.2
  • 32
    • 0036293744 scopus 로고    scopus 로고
    • Association of DNA polymerase μ (pol μ) with Ku and Ligase IV: Role for pol μ in end-joining double-strand break repair
    • Mahajan KN, Nick McElhinny SA, Mitchell BS, Ramsden DA. Association of DNA polymerase μ (pol μ) with Ku and Ligase IV: role for pol μ in end-joining double-strand break repair. Mol Cell Biol 2002;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
  • 33
    • 0031925532 scopus 로고    scopus 로고
    • Structure of nonhairpin coding-end DNA breaks in cells undergoing V(D)J recombination
    • Schlissel MS. Structure of nonhairpin coding-end DNA breaks in cells undergoing V(D)J recombination. Mol Cell Biol 1998;18:2029-2037.
    • (1998) Mol Cell Biol , vol.18 , pp. 2029-2037
    • Schlissel, M.S.1
  • 34
    • 0034714096 scopus 로고    scopus 로고
    • DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis
    • Garcia-Diaz M, et al. DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis. J Mol Biol 2000;301:851-867.
    • (2000) J Mol Biol , vol.301 , pp. 851-867
    • Garcia-Diaz, M.1
  • 35
    • 0034613393 scopus 로고    scopus 로고
    • Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta-related enzyme
    • Nagasawa K, et al. Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta-related enzyme. J Biol Chem 2000;275:31233-31238.
    • (2000) J Biol Chem , vol.275 , pp. 31233-31238
    • Nagasawa, K.1
  • 36
    • 0035860767 scopus 로고    scopus 로고
    • Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: A possible role in base excision repair
    • Garcia-Diaz M, Bebenek K, Kunkel TA, Blanco L. Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J Biol Chem 2001;276:34659-34663.
    • (2001) J Biol Chem , vol.276 , pp. 34659-34663
    • Garcia-Diaz, M.1    Bebenek, K.2    Kunkel, T.A.3    Blanco, L.4
  • 37
    • 0141483284 scopus 로고    scopus 로고
    • The frameshift infidelity of human DNA polymerase lambda. Implications for function
    • Bebenek K, Garcia-Diaz M, Blanco L, Kunkel TA. The frameshift infidelity of human DNA polymerase lambda. Implications for function. J Biol Chem 2003;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
  • 38
    • 0037066719 scopus 로고    scopus 로고
    • DNA polymerase lambda, a novel DNA repair enzyme in human cells
    • Garcia-Diaz M, et al. DNA polymerase lambda, a novel DNA repair enzyme in human cells. J Biol Chem 2002;277:13184-13191.
    • (2002) J Biol Chem , vol.277 , pp. 13184-13191
    • Garcia-Diaz, M.1
  • 39
    • 0347683431 scopus 로고    scopus 로고
    • Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts
    • Lee JW, et al. Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts. J Biol Chem 2004;279:805-811.
    • (2004) J Biol Chem , vol.279 , pp. 805-811
    • Lee, J.W.1
  • 40
    • 17944397758 scopus 로고    scopus 로고
    • Hydrocephalus, situs inversus, chronic sinusitis, and male infertility in DNA polymerase lambda-deficient mice: Possible implication for the pathogenesis of immotile cilia syndrome
    • Kobayashi Y, et al. Hydrocephalus, situs inversus, chronic sinusitis, and male infertility in DNA polymerase lambda-deficient mice: possible implication for the pathogenesis of immotile cilia syndrome. Mol Cell Biol 2002;22:2769-2776.
    • (2002) Mol Cell Biol , vol.22 , pp. 2769-2776
    • Kobayashi, Y.1
  • 41
    • 0037090311 scopus 로고    scopus 로고
    • Cutting edge: DNA polymerases mu and lambda are dispensable for Ig gene hypermutation
    • Bertocci B, et al. Cutting edge: DNA polymerases mu and lambda are dispensable for Ig gene hypermutation. J Immunol 2002;168:3702-3706.
    • (2002) J Immunol , vol.168 , pp. 3702-3706
    • Bertocci, B.1
  • 42
    • 0027983024 scopus 로고
    • P nucleotide insertions and the resolution of hairpin DNA structures in mammalian cells
    • Lewis SM. P nucleotide insertions and the resolution of hairpin DNA structures in mammalian cells. Proc Natl Acad Sci USA 1994;91:1332-1336.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1332-1336
    • Lewis, S.M.1
  • 43
    • 0032435650 scopus 로고    scopus 로고
    • TdT-accessible breaks are scattered over the immunoglobulin V domain in a constitutively hypermutating B cell line
    • Sale JE, Neuberger MS. TdT-accessible breaks are scattered over the immunoglobulin V domain in a constitutively hypermutating B cell line. Immunity 1998;9:859-869.
    • (1998) Immunity , vol.9 , pp. 859-869
    • Sale, J.E.1    Neuberger, M.S.2
  • 44
    • 0037160145 scopus 로고    scopus 로고
    • A physical and functional interaction between yeast Pol4 and Dnl4-Lif1 links DNA synthesis and ligation in nonhomologous end joining
    • Tseng HM, Tomkinson AE. A physical and functional interaction between yeast Pol4 and Dnl4-Lif1 links DNA synthesis and ligation in nonhomologous end joining. J Biol Chem 2002;277:45630-45637.
    • (2002) J Biol Chem , vol.277 , pp. 45630-45637
    • Tseng, H.M.1    Tomkinson, A.E.2
  • 45
    • 0037224429 scopus 로고    scopus 로고
    • Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro
    • Lee JW, Yannone SM, Chen DJ, Povirk LF. Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro. Cancer Res 2003;63:22-24.
    • (2003) Cancer Res , vol.63 , pp. 22-24
    • Lee, J.W.1    Yannone, S.M.2    Chen, D.J.3    Povirk, L.F.4
  • 46
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke IA, Lowery DM, Nguyen A, Yaffe MB. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 2003;302:636-639.
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 47
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X, Chini CC, He M, Mer G, Chen J. The BRCT domain is a phospho-protein binding domain. Science 2003;302:639-642.
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 48
    • 0346101743 scopus 로고    scopus 로고
    • Phosphopeptide binding specificities of BRCT domains
    • Rodriguez M, Yu X, Chen J, Songyang Z. Phosphopeptide binding specificities of BRCT domains. J Biol Chem 2003;278:52914-52918.
    • (2003) J Biol Chem , vol.278 , pp. 52914-52918
    • Rodriguez, M.1    Yu, X.2    Chen, J.3    Songyang, Z.4
  • 49
    • 0018823750 scopus 로고
    • Control of nucleotide pools in mammalian cells
    • Bjursell G, Skoog L. Control of nucleotide pools in mammalian cells. Antibiot Chemother 1980;28:78-85.
    • (1980) Antibiot Chemother , vol.28 , pp. 78-85
    • Bjursell, G.1    Skoog, L.2
  • 50
    • 0020611441 scopus 로고
    • Changes in ribo- and deoxyribonucleoside triphosphate pools within the cell cycle of a synchronized mouse fibroblast cell line
    • McCormick PJ, Danhauser LL, Rustum YM, Bertram JS. Changes in ribo- and deoxyribonucleoside triphosphate pools within the cell cycle of a synchronized mouse fibroblast cell line. Biochim Biophys Acta 1983;756:36-40.
    • (1983) Biochim Biophys Acta , vol.756 , pp. 36-40
    • McCormick, P.J.1    Danhauser, L.L.2    Rustum, Y.M.3    Bertram, J.S.4
  • 51
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata M, et al. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J 1998;17:5497-5508.
    • (1998) EMBO J , vol.17 , pp. 5497-5508
    • Takata, M.1
  • 52
    • 0042632901 scopus 로고    scopus 로고
    • Pathways of DNA double-strand break repair during the mammalian cell cycle
    • Rothkamm K, Kruger I, Thompson LH, Lobrich M. Pathways of DNA double-strand break repair during the mammalian cell cycle. Mol Cell Biol 2003;23:5706-5715.
    • (2003) Mol Cell Biol , vol.23 , pp. 5706-5715
    • Rothkamm, K.1    Kruger, I.2    Thompson, L.H.3    Lobrich, M.4
  • 53
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut TW. Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 1994;140:1-22.
    • (1994) Mol Cell Biochem , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 54
    • 0042662911 scopus 로고    scopus 로고
    • Lack of sugar discrimination by human Pol mu requires a single glycine residue
    • Ruiz JF, et al. Lack of sugar discrimination by human Pol mu requires a single glycine residue. Nucleic Acids Res 2003;31:4441-4449.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4441-4449
    • Ruiz, J.F.1
  • 55
    • 0014198528 scopus 로고
    • Deoxynucleotide-polymerizing enzymes of calf thymus gland. II. Properties of the terminal deoxynucleotidyltransferase
    • Kato KI, Goncalves JM, Houts GE, Bollum FJ. Deoxynucleotide-polymerizing enzymes of calf thymus gland. II. Properties of the terminal deoxynucleotidyltransferase. J Biol Chem 1967;242:2780-2789.
    • (1967) J Biol Chem , vol.242 , pp. 2780-2789
    • Kato, K.I.1    Goncalves, J.M.2    Houts, G.E.3    Bollum, F.J.4
  • 56
    • 0015223458 scopus 로고
    • Synthetic polynucleotides. Enzymic synthesis of ribonucleotide terminated oligodeoxynucleotides and their use as primers for the enzymic synthesis of polydeoxynucleotides
    • Roychoudhury R, Kossel H. Synthetic polynucleotides. Enzymic synthesis of ribonucleotide terminated oligodeoxynucleotides and their use as primers for the enzymic synthesis of polydeoxynucleotides. Eur J Biochem 1971;22:310-320.
    • (1971) Eur J Biochem , vol.22 , pp. 310-320
    • Roychoudhury, R.1    Kossel, H.2
  • 57
    • 0015523261 scopus 로고
    • Enzymic synthesis of polynucleotides. Oligodeoxynucleotides with one 3′-terminal ribonucleotide as primers for polydeoxynucleotide synthesis
    • Roychoudhury R. Enzymic synthesis of polynucleotides. Oligodeoxynucleotides with one 3′-terminal ribonucleotide as primers for polydeoxynucleotide synthesis. J Biol Chem 1972;247:3910-3917.
    • (1972) J Biol Chem , vol.247 , pp. 3910-3917
    • Roychoudhury, R.1
  • 58
    • 0035903113 scopus 로고    scopus 로고
    • Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides
    • Boule JB, Rougeon F, Papanicolaou C. Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. J Biol Chem 2001;276:31388-31393.
    • (2001) J Biol Chem , vol.276 , pp. 31388-31393
    • Boule, J.B.1    Rougeon, F.2    Papanicolaou, C.3
  • 59
    • 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 2002;99:16654-16659.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16654-16659
    • Rydberg, B.1    Game, J.2
  • 60
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
    • Pelletier H, Sawaya MR, Kumar A, Wilson SH, Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP. Science 1994;264:1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 61
    • 0027273727 scopus 로고
    • Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase
    • Doyen N, d'Andon MF, Bentolila LA, Nguyen QT, Rougeon F. Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase. Nucleic Acids Res 1993;21:1187-1191.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1187-1191
    • Doyen, N.1    D'Andon, M.F.2    Bentolila, L.A.3    Nguyen, Q.T.4    Rougeon, F.5
  • 62
    • 0023056869 scopus 로고
    • Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells
    • Koiwai O, Yokota T, Kageyama T, Hirose T, Yoshida S, Arai K. Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells. Nucleic Acids Res 1986;14:5777-5792.
    • (1986) Nucleic Acids Res , vol.14 , pp. 5777-5792
    • Koiwai, O.1    Yokota, T.2    Kageyama, T.3    Hirose, T.4    Yoshida, S.5    Arai, K.6
  • 63
    • 0036091560 scopus 로고    scopus 로고
    • Distinct and opposite diversifying activities of terminal transferase splice variants
    • Thai TH, Purugganan MM, Roth DB, Kearney JF. Distinct and opposite diversifying activities of terminal transferase splice variants. Nat Immunol 2002;3:457-462.
    • (2002) Nat Immunol , vol.3 , pp. 457-462
    • Thai, T.H.1    Purugganan, M.M.2    Roth, D.B.3    Kearney, J.F.4
  • 64
    • 0029155451 scopus 로고
    • The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization
    • Bentolila LA, Fanton d'Andon M, Nguyen QT, Martinez O, Rougeon F, Doyen N. The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization. EMBO J 1995;14:4221-4229.
    • (1995) EMBO J , vol.14 , pp. 4221-4229
    • Bentolila, L.A.1    Fanton D'Andon, M.2    Nguyen, Q.T.3    Martinez, O.4    Rougeon, F.5    Doyen, N.6
  • 65
    • 0035180391 scopus 로고    scopus 로고
    • The long isoform of terminal deoxynucleotidyl transferase enters the nucleus and, rather than catalyzing nontemplated nucleotide addition, modulates the catalytic activity of the short isoform
    • Benedict CL, Gilfillan S, Kearney JF. The long isoform of terminal deoxynucleotidyl transferase enters the nucleus and, rather than catalyzing nontemplated nucleotide addition, modulates the catalytic activity of the short isoform. J Exp Med 2001;193:89-99.
    • (2001) J Exp Med , vol.193 , pp. 89-99
    • Benedict, C.L.1    Gilfillan, S.2    Kearney, J.F.3
  • 66
    • 0034664728 scopus 로고    scopus 로고
    • Comparison of the two murine terminal [corrected] deoxynucleotidyltransferase terminal isoforms. A 20-amino acid insertion in the highly conserved carboxyl-terminal region modifies the thermosensitivity but not the catalytic activity
    • Boule JB, Rougeon F, Papanicolaou C. Comparison of the two murine terminal [corrected] deoxynucleotidyltransferase terminal isoforms. A 20-amino acid insertion in the highly conserved carboxyl-terminal region modifies the thermosensitivity but not the catalytic activity. J Biol Chem 2000;275:28984-28988.
    • (2000) J Biol Chem , vol.275 , pp. 28984-28988
    • Boule, J.B.1    Rougeon, F.2    Papanicolaou, C.3
  • 67
    • 0036469941 scopus 로고    scopus 로고
    • Crystal structures of a template-independent DNA polymerase: Murine terminal deoxynucleotidyltransferase
    • Delarue M, et al. Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase. EMBO J 2002;21:427-439.
    • (2002) EMBO J , vol.21 , pp. 427-439
    • Delarue, M.1
  • 69
    • 0020354447 scopus 로고
    • Sites and structure of gamma radiation-induced DNA strand breaks
    • Henner WD, Grunberg SM, Haseltine WA. Sites and structure of gamma radiation-induced DNA strand breaks. J Biol Chem 1982;257:11750-11754.
    • (1982) J Biol Chem , vol.257 , pp. 11750-11754
    • Henner, W.D.1    Grunberg, S.M.2    Haseltine, W.A.3
  • 70
    • 0037113885 scopus 로고    scopus 로고
    • Lesion bypass activities of human DNA polymerase mu
    • Zhang Y, et al. Lesion bypass activities of human DNA polymerase mu. J Biol Chem 2002;277:44582-44587.
    • (2002) J Biol Chem , vol.277 , pp. 44582-44587
    • Zhang, Y.1
  • 71
    • 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, Livneh Z. Lesion bypass by human DNA polymerase mu reveals a template-dependent sequence-independent nucleotidyl transferase activity. J Biol Chem 2004;279:859-865.
    • (2004) J Biol Chem , vol.279 , pp. 859-865
    • Covo, S.1    Blanco, L.2    Livneh, Z.3
  • 72
    • 0037166307 scopus 로고    scopus 로고
    • DNA polymerase lambda from calf thymus preferentially replicates damaged DNA
    • Ramadan K, Shevelev IV, Maga G, Hubscher U. DNA polymerase lambda from calf thymus preferentially replicates damaged DNA. J Biol Chem 2002;277:18454-18458.
    • (2002) J Biol Chem , vol.277 , pp. 18454-18458
    • Ramadan, K.1    Shevelev, I.V.2    Maga, G.3    Hubscher, U.4
  • 73
    • 2242420935 scopus 로고    scopus 로고
    • Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis
    • Maga G, et al. Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis. J Biol Chem 2002;277:48434-48440.
    • (2002) J Biol Chem , vol.277 , pp. 48434-48440
    • Maga, G.1
  • 74
    • 0022512870 scopus 로고
    • Molecular biology of terminal transferase
    • Chang LM, Bollum FJ. Molecular biology of terminal transferase. CRC Crit Rev Biochem 1986;21:27-52.
    • (1986) CRC Crit Rev Biochem , vol.21 , pp. 27-52
    • Chang, L.M.1    Bollum, F.J.2
  • 75
    • 0032529448 scopus 로고    scopus 로고
    • DNA synthesis on discontinuous templates by human DNA polymerases: Implications for non-homologous DNA recombination
    • Islas L, Fairley CF, Morgan WF. DNA synthesis on discontinuous templates by human DNA polymerases: implications for non-homologous DNA recombination. Nucleic Acids Res 1998;26:3729-3738.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3729-3738
    • Islas, L.1    Fairley, C.F.2    Morgan, W.F.3
  • 76
    • 0035420079 scopus 로고    scopus 로고
    • The role of DNA polymerase activity in human non-homologous end joining
    • Pospiech H, Rytkonen AK, Syvaoja JE. The role of DNA polymerase activity in human non-homologous end joining. Nucleic Acids Res 2001;29:3277-3288.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3277-3288
    • Pospiech, H.1    Rytkonen, A.K.2    Syvaoja, J.E.3
  • 77
    • 0035985037 scopus 로고    scopus 로고
    • Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme
    • Shimazaki N, Yoshida K, Kobayashi T, Toji S, Tamai K, Koiwai O. Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme. Genes Cells 2002;7:639-651.
    • (2002) Genes Cells , vol.7 , pp. 639-651
    • Shimazaki, N.1    Yoshida, K.2    Kobayashi, T.3    Toji, S.4    Tamai, K.5    Koiwai, O.6
  • 78
    • 0034820561 scopus 로고    scopus 로고
    • Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen
    • Ibe S, et al. Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen. Genes Cells 2001;6:815-824.
    • (2001) Genes Cells , vol.6 , pp. 815-824
    • Ibe, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.