메뉴 건너뛰기




Volumn 32, Issue 7, 2004, Pages 2193-2201

XRCC1 co-localizes and physically interacts with PCNA

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLINE; DNA; POLYPEPTIDE; PROTEIN XRCC1; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; CELL EXTRACT; DNA BINDING PROTEIN; X RAY REPAIR CROSS COMPLEMENTING PROTEIN 1; X-RAY REPAIR CROSS COMPLEMENTING PROTEIN 1;

EID: 2342627913     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh556     Document Type: Article
Times cited : (168)

References (53)
  • 1
    • 0019956767 scopus 로고
    • A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair and an extraordinary baseline frequency of sister-chromatid exchange
    • Thompson,L.H., Brookman,K.W., Dillehay,L.E., Carrano,A.V., Mazrimas,J.A., Mooney,C.L. and Minkler,J.L. (1982) A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair and an extraordinary baseline frequency of sister-chromatid exchange. Murat. Res., 95, 427-440.
    • (1982) Mutat. Res. , vol.95 , pp. 427-440
    • 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
  • 2
    • 0021252418 scopus 로고
    • DNA-strand breaks associated with halogenated pyrimidine incorporation
    • Dillehay,L.E., Thompson,L.H. and Carrano,A.V. (1984) DNA-strand breaks associated with halogenated pyrimidine incorporation. Mutat. Res., 131, 129-136.
    • (1984) Mutat. Res. , vol.131 , pp. 129-136
    • Dillehay, L.E.1    Thompson, L.H.2    Carrano, A.V.3
  • 3
    • 0025202114 scopus 로고
    • Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • Thompson,L.H., Brookman,K.W., Jones,N.J., Allen,S.A. and Carrano,A.V. (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
  • 5
    • 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., Aoufouchi,S., Johnson,P. and Shall,S. (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
  • 6
    • 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., Nash,R.A., Klungland,A., Schar,P., Barnes,D.E. and Lindahl,T. (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
  • 8
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions
    • Vidal,A.E., Boiteux,S., Hickson,I.D. and Radicella,J.P. (2001) XRCC1 coordinates the initial and late stages of DNA abasic site repair through 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
  • 10
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo,I., Liao,Z.Y., Barcelo,J.M., Kohlhagen,G., Caldecott,K.W., Weinfeld,M. and Pommier,Y. (2003) Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair (Amst.), 2, 1087-1100.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1087-1100
    • Plo, I.1    Liao, Z.Y.2    Barcelo, J.M.3    Kohlhagen, G.4    Caldecott, K.W.5    Weinfeld, M.6    Pommier, Y.7
  • 11
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson,M., Niedergang,C., Schreiber,V., Muller,S., Menissier-de Murcia,J. and de Murcia,G. (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    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 12
    • 0037151051 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
    • Schreiber,V., Ame,J.C., Dolle,P., Schultz,I., Rinaldi,B., Fraulob,V., Menissier-de Murcia,J. and de Murcia,G. (2002) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem., 277, 23028-23036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Ame, J.C.2    Dolle, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6    Menissier-de Murcia, J.7    de Murcia, G.8
  • 14
    • 0034694841 scopus 로고    scopus 로고
    • The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature
    • Yamane,K., Katayama,E. and Tsuruo,T. (2000) The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature. Biochem. Biophys. Res. Commun., 279, 678-684.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 678-684
    • Yamane, K.1    Katayama, E.2    Tsuruo, T.3
  • 15
    • 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., Moore,D.J., Whitehouse,J., Johnson,P. and Caldecott,K.W. (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
  • 16
    • 0037414338 scopus 로고    scopus 로고
    • Independent roles of XRCC1's two BRCT motifs in recovery from methylation damage
    • Kubota,Y. and Horiuchi,S. (2003) Independent roles of XRCC1's two BRCT motifs in recovery from methylation damage. DNA Repair (Amst.), 2, 407-415.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 407-415
    • Kubota, Y.1    Horiuchi, S.2
  • 17
    • 0036208101 scopus 로고    scopus 로고
    • Central role for the XRCC1 BRCT I domain in mammalian DNA single-strand break repair
    • Taylor,R.M., Thistlethwaite,A. and Caldecott,K.W. (2002) Central role for the XRCC1 BRCT I domain in mammalian DNA single-strand break repair. Mol. Cell. Biol., 22, 2556-2563.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2556-2563
    • Taylor, R.M.1    Thistlethwaite, A.2    Caldecott, K.W.3
  • 19
    • 0026550033 scopus 로고
    • Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions
    • Matyus,L. (1992) Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions. J. Photochem. Photobiol. B, 12, 323-337.
    • (1992) J. Photochem. Photobiol. B. , vol.12 , pp. 323-337
    • Matyus, L.1
  • 20
    • 0141480945 scopus 로고    scopus 로고
    • WRN interacts physically and functionally with the recombination mediator protein RAD52
    • Baynton,K., Otterlei,M., Bjoras,M., von Kobbe,C., Bohr,V.A. and Seeberg,E. (2003) WRN interacts physically and functionally with the recombination mediator protein RAD52. J. Biol. Chem., 278, 36476-36486.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36476-36486
    • Baynton, K.1    Otterlei, M.2    Bjoras, M.3    von Kobbe, C.4    Bohr, V.A.5    Seeberg, E.6
  • 21
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia,Z. and Liu,Y. (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J., 81, 2395-2402.
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 22
    • 0030692134 scopus 로고    scopus 로고
    • An interaction between DNA ligase I and proliferating cell nuclear antigen: Implications for Okazaki fragment synthesis and joining
    • Levin,D.S., Bai,W., Yao,N., O'Donnell,M. and Tomkinson,A.E. (1997) An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining. Proc. Natl Acad. Sci. USA, 94, 12863-12868.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12863-12868
    • Levin, D.S.1    Bai, W.2    Yao, N.3    O'Donnell, M.4    Tomkinson, A.E.5
  • 23
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • Erzberger,J.P., Barsky,D., Scharer,O.D., Colvin,M.E. and Wilson,D.M.,III (1998) Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases. Nucleic Acids Res., 26, 2771-2778.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2771-2778
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson III, D.M.5
  • 24
    • 0034607548 scopus 로고    scopus 로고
    • Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease
    • Nguyen,L.H., Barsky,D., Erzberger,J.P. and Wilson,D.M.,III (2000) Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease. J. Mol. Biol., 298, 447-459.
    • (2000) J. Mol. Biol. , vol.298 , pp. 447-459
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson III, D.M.4
  • 25
    • 0033621353 scopus 로고    scopus 로고
    • The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities
    • Lee,B.I. and Wilson,D.M.,III (1999) The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities. J. Biol. Chem., 274, 37763-37769.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37763-37769
    • Lee, B.I.1    Wilson III, D.M.2
  • 26
    • 0038583869 scopus 로고    scopus 로고
    • Spatial and temporal cellular responses to single-strand breaks in human cells
    • Okano,S., Lan,L., Caldecott,K.W., Mori,T. and Yasui,A. (2003) Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol., 23, 3974-3981.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5
  • 27
    • 0022039158 scopus 로고
    • Changes in the nuclear distribution of cyclin (PCNA) but not its synthesis depend on DNA replication
    • Bravo,R. and Macdonald-Bravo,H. (1985) Changes in the nuclear distribution of cyclin (PCNA) but not its synthesis depend on DNA replication. EMBO J., 4, 655-661.
    • (1985) EMBO J. , vol.4 , pp. 655-661
    • Bravo, R.1    Macdonald-Bravo, H.2
  • 28
    • 0010697057 scopus 로고
    • Cell cycle-dependent variations in the distribution of the nuclear protein cyclin proliferating cell nuclear antigen in cultured cells: Subdivision of S phase
    • Celis,J.E. and Celis,A. (1985) Cell cycle-dependent variations in the distribution of the nuclear protein cyclin proliferating cell nuclear antigen in cultured cells: subdivision of S phase. Proc. Natl Acad. Sci. USA, 82, 3262-3266.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3262-3266
    • Celis, J.E.1    Celis, A.2
  • 29
    • 0023091938 scopus 로고
    • Functional identity of proliferating cell nuclear antigen and a DNA polymerase-delta auxiliary protein
    • Prelich,G., Tan,C.K., Kostura,M., Mathews,M.B., So,A.G., Downey,K.M. and Stillman,B. (1987) Functional identity of proliferating cell nuclear antigen and a DNA polymerase-delta auxiliary protein. Nature, 326, 517-520.
    • (1987) Nature , vol.326 , pp. 517-520
    • Prelich, G.1    Tan, C.K.2    Kostura, M.3    Mathews, M.B.4    So, A.G.5    Downey, K.M.6    Stillman, B.7
  • 30
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick,E. (2000) The puzzle of PCNA's many partners. Bioessays, 22, 997-1006.
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 31
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga,G. and Hubscher,U. (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci., 116, 3051-3060.
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 33
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar,R.B. and Periasamy,A. (2003) Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol., 160, 629-633.
    • (2003) J. Cell Biol. , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 34
    • 0028132878 scopus 로고
    • Trimeric structure of human proliferating cell nuclear antigen. Implications for enzymatic function and autoantibody recognition
    • Brand,S.R., Bernstein,R.M. and Mathews,M.B. (1994) Trimeric structure of human proliferating cell nuclear antigen. Implications for enzymatic function and autoantibody recognition. J. Immunol., 153, 3070-3078.
    • (1994) J. Immunol. , vol.153 , pp. 3070-3078
    • Brand, S.R.1    Bernstein, R.M.2    Mathews, M.B.3
  • 37
    • 0037440184 scopus 로고    scopus 로고
    • Site-directed mutagenesis analysis of the structural interaction of the single-strand-break repair protein, X-ray cross-complementing group 1, with DNA polymerase β
    • Marintchev,A., Gryk,MR. and Mullen,G.P. (2003) Site-directed mutagenesis analysis of the structural interaction of the single-strand-break repair protein, X-ray cross-complementing group 1, with DNA polymerase β. Nucleic Acids Res., 31, 580-588.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 580-588
    • Marintchev, A.1    Gryk, M.R.2    Mullen, G.P.3
  • 38
    • 0029949916 scopus 로고    scopus 로고
    • S phase specific formation of the human Rad51 protein nuclear foci in lymphocytes
    • Tashiro,S., Kotomura,N., Shinohara,A., Tanaka,K., Ueda,K. and Kamada,N. (1996) S phase specific formation of the human Rad51 protein nuclear foci in lymphocytes. Oncogene, 12, 2165-2170.
    • (1996) Oncogene , vol.12 , pp. 2165-2170
    • Tashiro, S.1    Kotomura, N.2    Shinohara, A.3    Tanaka, K.4    Ueda, K.5    Kamada, N.6
  • 40
    • 0033955346 scopus 로고    scopus 로고
    • XRCC1 keeps DNA from getting stranded
    • Thompson,L.H. and West,M.G. (2000) XRCC1 keeps DNA from getting stranded. Mutat. Res., 459, 1-18.
    • (2000) Mutat. Res. , vol.459 , pp. 1-18
    • Thompson, L.H.1    West, M.G.2
  • 41
    • 0027134511 scopus 로고
    • Abnormally high incidence of SCE in three successive cell cycles in the CHO mutant EM9 as detected by a three-way immunoperoxidase differential staining
    • Pinero,J. and Cortes,F. (1993) Abnormally high incidence of SCE in three successive cell cycles in the CHO mutant EM9 as detected by a three-way immunoperoxidase differential staining. Mutat. Res., 292, 205-211.
    • (1993) Mutat. Res. , vol.292 , pp. 205-211
    • Pinero, J.1    Cortes, F.2
  • 42
    • 0035853295 scopus 로고    scopus 로고
    • DNA double-strand breaks associated with replication forks are predominantly repaired by homologous recombination involving an exchange mechanism in mammalian cells
    • Arnaudeau,C., Lundin,C. and Helleday,T. (2001) DNA double-strand breaks associated with replication forks are predominantly repaired by homologous recombination involving an exchange mechanism in mammalian cells. J. Mol. Biol., 307, 1235-1245.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1235-1245
    • Arnaudeau, C.1    Lundin, C.2    Helleday, T.3
  • 43
    • 0344875495 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination
    • Schultz,N., Lopez,E., Saleh-Gohari,N. and Helleday,T. (2003) Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination. Nucleic Acids Res., 31, 4959-4964.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4959-4964
    • Schultz, N.1    Lopez, E.2    Saleh-Gohari, N.3    Helleday, T.4
  • 45
    • 0032522224 scopus 로고    scopus 로고
    • Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: A link between DNA strand break detection and DNA replication
    • Dantzer,F., Nasheuer,H.P., Vonesch,J.L., de Murcia,G. and Menissier-de Murcia,J. (1998) Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication. Nucleic Acids Res., 26, 1891-1898.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1891-1898
    • Dantzer, F.1    Nasheuer, H.P.2    Vonesch, J.L.3    de Murcia, G.4    Menissier-de Murcia, J.5
  • 46
    • 0141960298 scopus 로고    scopus 로고
    • Human proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1 and p21waf1/cip1. A dynamic exchange of partners
    • Frouin,I., Maga,G., Denegri,M., Riva,F., Savio,M., Spadari,S., Prosperi,E. and Scovassi,A.I. (2003) Human proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1 and p21waf1/cip1. A dynamic exchange of partners. J. Biol. Chem., 278, 39265-39268.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39265-39268
    • Frouin, I.1    Maga, G.2    Denegri, M.3    Riva, F.4    Savio, M.5    Spadari, S.6    Prosperi, E.7    Scovassi, A.I.8
  • 48
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El Khamisy,S.F., Masutani,M., Suzuki,H. and Caldecott,K.W. (2003) A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res., 31, 5526-5533.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 50
    • 0036198664 scopus 로고    scopus 로고
    • DNA mismatch repair and mutation avoidance pathways
    • Marti,T.M., Kunz,C. and Fleck,O. (2002) DNA mismatch repair and mutation avoidance pathways. J. Cell. Physiol., 191, 28-41.
    • (2002) J. Cell. Physiol. , vol.191 , pp. 28-41
    • Marti, T.M.1    Kunz, C.2    Fleck, O.3
  • 53
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott,K.W. (2003) XRCC1 and DNA strand break repair. DNA Repair (Amst.), 2, 955-969.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 955-969
    • Caldecott, K.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.