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Volumn 23, Issue 16, 2003, Pages 5919-5927

Physical and functional interaction between DNA ligase IIIα and poly(ADP-ribose) polymerase 1 in DNA single-strand break repair

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE 3ALPHA; PROTEIN; PROTEIN XRCC1; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 0042632806     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.16.5919-5927.2003     Document Type: Article
Times cited : (200)

References (36)
  • 2
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase β and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular nick-sensor in vitro
    • Caldecott, K. W., S. Aoufouchi, P. Johnson, and S. Shall. 1996. XRCC1 polypeptide interacts with DNA polymerase β and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular nick-sensor in vitro. Nucleic Acids Res. 24:4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 4
    • 0028862933 scopus 로고    scopus 로고
    • Characterization of the Xrcc1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • Caldecott, K. W., C. K. McKeown, J. D. Tucker, L. Stanker, and L. H. Thompson. 1996. Characterization of the Xrcc1-DNA ligase III complex in vitro and its absence from mutant hamster cells. Nucleic Acids Res. 23:4836-4843.
    • (1996) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    McKeown, C.K.2    Tucker, J.D.3    Stanker, L.4    Thompson, L.H.5
  • 5
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAP1: A widespread BRCT module closely associated with DNA repair
    • Callebaut, I., and J. P. Mornon. 1997. From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair. FEBS Lett. 400:25-30.
    • (1997) FEBS Lett. , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.P.2
  • 7
    • 0000102949 scopus 로고
    • Poly(ADP) ribose polymerase: A molecular nick sensor
    • de Murcia, G., and J. Menissier-de Murcia. 1994. Poly(ADP) ribose polymerase: a molecular nick sensor. Trends Biochem. Sci. 19:172-176.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 172-176
    • De Murcia, G.1    Menissier-de Murcia, J.2
  • 9
    • 0026659182 scopus 로고
    • Overproduction and large scale purification of human poly (ADP-ribose) polymerase using a baculovirus expression system
    • Giner, H., F. Simonin, G. de Murcia, and J. Menissier-de Murcia. 1992. Overproduction and large scale purification of human poly (ADP-ribose) polymerase using a baculovirus expression system. Gene 11:279-283.
    • (1992) Gene , vol.11 , pp. 279-283
    • Giner, H.1    Simonin, F.2    De Murcia, G.3    Menissier-de Murcia, J.4
  • 12
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubota, Y., R. A. Nash, A. Klungland, P. Schar, D. E. Barnes, and T. Lindahl. 1996. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein. EMBO J. 15:6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0032960864 scopus 로고    scopus 로고
    • The human DNA ligase III gene encodes nuclear and mitochondrial proteins
    • Lakshmipathy, U., and C. Campbell. 1999. The human DNA ligase III gene encodes nuclear and mitochondrial proteins. Mol. Cell. Biol. 19:3869-3876.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3869-3876
    • Lakshmipathy, U.1    Campbell, C.2
  • 15
    • 0034667766 scopus 로고    scopus 로고
    • Mitochondrial DNA ligase III function is independent of Xrcc1
    • Lakshmipathy, U., and C. Campbell. 2000. Mitochondrial DNA ligase III function is independent of Xrcc1. Nucleic Acids Res. 28:3880-3886.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3880-3886
    • Lakshmipathy, U.1    Campbell, C.2
  • 16
    • 0033618289 scopus 로고    scopus 로고
    • DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III
    • Mackey, Z. B., C. Niedergang, J. M. Murcia, J. Leppard, K. Au, J. Chen, G. de Murcia, and A. E. Tomkinson. 1999. DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III. J. Biol. Chem. 274:21679-21687.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21679-21687
    • Mackey, Z.B.1    Niedergang, C.2    Murcia, J.M.3    Leppard, J.4    Au, K.5    Chen, J.6    De Murcia, G.7    Tomkinson, A.E.8
  • 17
    • 0031045858 scopus 로고    scopus 로고
    • An alternative splicing event, which occurs in mouse pachytene spermatocytes, generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination
    • Mackey, Z. B., W. Ramos, D. S. Levin, C. A. Walter, J. R. McCarrey, and A. E. Tomkinson. 1996. An alternative splicing event, which occurs in mouse pachytene spermatocytes, generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination. Mol. Cell. Biol. 17:989-998.
    • (1996) Mol. Cell. Biol. , vol.17 , pp. 989-998
    • Mackey, Z.B.1    Ramos, W.2    Levin, D.S.3    Walter, C.A.4    McCarrey, J.R.5    Tomkinson, A.E.6
  • 19
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson, M., C. Niedergang, V. Schreiebr, S. Muller, J. Menissier de Murcia, and G. de Murcia. 1998. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18:3563-3571.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiebr, V.3    Muller, S.4    Menissier de Murcia, J.5    De Murcia, G.6
  • 20
    • 0034610276 scopus 로고    scopus 로고
    • Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells
    • Moore, D. J., R. M. Taylor, P. Clements, and K. W. Caldecott. 2000. Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 97:13649-13654.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13649-13654
    • Moore, D.J.1    Taylor, R.M.2    Clements, P.3    Caldecott, K.W.4
  • 21
    • 0030941295 scopus 로고    scopus 로고
    • XRCC1 protein interacts with one of two distinct forms of DNA ligase III
    • Nash, R. A., K. Caldecott, D. E. Barnes, and T. Lindahl. 1997. XRCC1 protein interacts with one of two distinct forms of DNA ligase III. Biochemistry 36:5207-5211.
    • (1997) Biochemistry , vol.36 , pp. 5207-5211
    • Nash, R.A.1    Caldecott, K.2    Barnes, D.E.3    Lindahl, T.4
  • 22
    • 0035966099 scopus 로고    scopus 로고
    • Two forms of mitochondrial DNA ligase III are produced in Xenopus laevis oocytes
    • Perez-Jannotti, R. M., S. M. Klein, and D. F. Bogenhagen. 2001. Two forms of mitochondrial DNA ligase III are produced in Xenopus laevis oocytes. J. Biol. Chem. 276:48978-48987.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48978-48987
    • Perez-Jannotti, R.M.1    Klein, S.M.2    Bogenhagen, D.F.3
  • 23
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in checkpoint proteins
    • Pleschke, J. M., H. E. Kleczkowska, M. Strohm, and F. R. Althaus. 2000. Poly(ADP-ribose) binds to specific domains in checkpoint proteins. J. Biol. Chem. 275:40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 24
    • 0027052982 scopus 로고
    • pGSTag - A versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins
    • Ron, D., and H. Dressler. 1992. pGSTag - a versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins. BioTechniques 13:866-868.
    • (1992) BioTechniques , vol.13 , pp. 866-868
    • Ron, D.1    Dressler, H.2
  • 25
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh, M., and T. Lindahl. 1992. Role of poly(ADP-ribose) formation in DNA repair. Nature 356:356-358.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.1    Lindahl, T.2
  • 26
  • 27
    • 0033976049 scopus 로고    scopus 로고
    • A cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repair
    • Taylor, R. M., D. J. Moore, J. Whitehouse, P. Johnson, and K. W. Caldecott. 2000. A cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repair. Mol. Cell. Biol. 20:735-740.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 735-740
    • Taylor, R.M.1    Moore, D.J.2    Whitehouse, J.3    Johnson, P.4    Caldecott, K.W.5
  • 28
    • 0019956767 scopus 로고
    • A CHO-cell strain having hypersensitivity to mutagens, a defect in strand break repair, and an extraordinary baseline frequency of sister chromatid exchange
    • Thompson, L. H., K. W. Brookman, L. E. Dillehay, A. V. Carrano, J. A. Mazrimas, C. L. Mooney, and J. L. Minkler. 1982. A CHO-cell strain having hypersensitivity to mutagens, a defect in strand break repair, and an extraordinary baseline frequency of sister chromatid exchange. Mutat. Res. 95:247-254.
    • (1982) Mutat. Res. , vol.95 , pp. 247-254
    • Thompson, L.H.1    Brookman, K.W.2    Dillehay, L.E.3    Carrano, A.V.4    Mazrimas, J.A.5    Mooney, C.L.6    Minkler, J.L.7
  • 29
    • 0025202114 scopus 로고
    • Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • Thompson, L. H., K. W. Brookman, N. J. Jones, S. A. Allen, and A. V. Carrano. 1990. Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Mol. Cell. Biol. 10:6160-6171.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6160-6171
    • Thompson, L.H.1    Brookman, K.W.2    Jones, N.J.3    Allen, S.A.4    Carrano, A.V.5
  • 30
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson, A. E., and Z. B. Mackey. 1998. Structure and function of mammalian DNA ligases. Mutat. Res. 407:1-9.
    • (1998) Mutat. Res. , vol.407 , pp. 1-9
    • Tomkinson, A.E.1    Mackey, Z.B.2
  • 31
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair though protein-protein interactions
    • Vidal, A. E., S. Boiteux, I. D. Hickson, and J. P. Radicella. 2001. XRCC1 coordinates the initial and late stages of DNA abasic site repair though protein-protein interactions. EMBO J. 20:6530-6539.
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 35
    • 0020200025 scopus 로고
    • A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase
    • Zahradka, P., and K. Ebisuzaki. 1982. A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase. Eur. J. Biochem. 127:579-585.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 579-585
    • Zahradka, P.1    Ebisuzaki, K.2
  • 36
    • 0026651211 scopus 로고
    • A Chinese hamster ovary cell mutant (EMC-11) with sensitivity to simple alkylating agents and a very high level of sister chromatid exchanges
    • Zdzienicka, M. Z., G. P. Vanderschans, A. T. Natarajan, L. H. Thompson, I. Neuteboom, and J. W. I. M. Simmons. 1992. A Chinese hamster ovary cell mutant (EMC-11) with sensitivity to simple alkylating agents and a very high level of sister chromatid exchanges. Mutagenesis 7:265-269.
    • (1992) Mutagenesis , vol.7 , pp. 265-269
    • Zdzienicka, M.Z.1    Vanderschans, G.P.2    Natarajan, A.T.3    Thompson, L.H.4    Neuteboom, I.5    Simmons, J.W.I.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.