메뉴 건너뛰기




Volumn 43, Issue 51, 2004, Pages 16505-16514

Biophysical characterization of human XRCC1 and its binding to damaged and undamaged DNA

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BINDING ENERGY; CONCENTRATION (PROCESS); ESCHERICHIA COLI; FLUORESCENCE; GENETIC ENGINEERING; PROTEINS; SEDIMENTATION; STOICHIOMETRY; TITRATION;

EID: 11144349584     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048615m     Document Type: Article
Times cited : (55)

References (52)
  • 1
    • 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
  • 3
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott, K. W. (2003) XRCC1 and DNA strand break repair, DNA Repair (Amsterdam) 2, 955-969.
    • (2003) DNA Repair (Amsterdam) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 4
    • 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
  • 5
    • 0012366228 scopus 로고    scopus 로고
    • Alkylating agents
    • (Chabner, B. A., and Longo, D. L., Ed.), Lippincott Williams and Wilkins, Philadelphia, PA
    • Tew, K. D., Colvin, O. M., and Chabner, B. A. (2001) Alkylating Agents, in Cancer Chemotherapy and Biotherapy: Principles and Practices (Chabner, B. A., and Longo, D. L., Ed.) pp 373-414, Lippincott Williams and Wilkins, Philadelphia, PA.
    • (2001) Cancer Chemotherapy and Biotherapy: Principles and Practices , pp. 373-414
    • Tew, K.D.1    Colvin, O.M.2    Chabner, B.A.3
  • 6
    • 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., Taylor, R. M., Clements, P., and Caldecott, K. W. (2000) Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells, Proc. Natl. Acad. Sci. U.S.A. 97, 13649-13654.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13649-13654
    • Moore, D.J.1    Taylor, R.M.2    Clements, P.3    Caldecott, K.W.4
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase beta 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 beta 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
  • 10
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase beta 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 beta 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
  • 12
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair
    • Whitehouse, C. J., Taylor, R. M., Thistlethwaite, A., Zhang, H., Karimi-Busheri, F., Lasko, D. D., Weinfeld, M., and Caldecott, K. W. (2001) XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair, Cell 104, 107-117.
    • (2001) Cell , vol.104 , pp. 107-117
    • Whitehouse, C.J.1    Taylor, R.M.2    Thistlethwaite, A.3    Zhang, H.4    Karimi-Busheri, F.5    Lasko, D.D.6    Weinfeld, M.7    Caldecott, K.W.8
  • 13
    • 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
  • 15
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork, P., Hofmann, K., Bucher, P., Neuwald, A. F., Altschul, S. F., and Koonin, E. V. (1997) A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins, FASEB J. 11, 68-76.
    • (1997) FASEB J. , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 16
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAP1: A widespread BRCT module closely associated with DNA repair
    • Callebaut, I., and Mornon, J. P. (1997) From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair, FEES Lett. 400, 25-30.
    • (1997) FEES Lett. , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.P.2
  • 18
    • 0030941295 scopus 로고    scopus 로고
    • XRCC1 protein interacts with one of two distinct forms of DNA ligase III
    • Nash, R. A., Caldecott, K. W., Barnes, D. E., and Lindahl, T. (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.W.2    Barnes, D.E.3    Lindahl, T.4
  • 19
    • 0032537747 scopus 로고    scopus 로고
    • Role of a BRCT domain in the interaction of DNA ligase III-alpha with the DNA repair protein XRCC1
    • Taylor, R. M., Wickstead, B., Cronin, S., and Caldecott, K. W. (1998) Role of a BRCT domain in the interaction of DNA ligase III-alpha with the DNA repair protein XRCC1, Curr. Biol. 8, 877-880.
    • (1998) Curr. Biol. , vol.8 , pp. 877-880
    • Taylor, R.M.1    Wickstead, B.2    Cronin, S.3    Caldecott, K.W.4
  • 22
    • 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
  • 24
    • 0028862933 scopus 로고
    • Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • Caldecott, K. W., Tucker, J. D., Stanker, L. H., and Thompson, L. H. (1995) Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells, Nucleic Acids Res. 23, 4836-4843.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    Tucker, J.D.2    Stanker, L.H.3    Thompson, L.H.4
  • 25
    • 0014663430 scopus 로고
    • Measurement of protein concentration with interferences optics
    • Babul, J., and Stellwagen, E. (1969) Measurement of protein concentration with interferences optics, Anal. Biochem. 28, 216-221.
    • (1969) Anal. Biochem. , vol.28 , pp. 216-221
    • Babul, J.1    Stellwagen, E.2
  • 26
  • 29
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M. L., Correia, J. J., Yphantis, D. A., and Halvorson, H. R. (1981) Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques, Biophys. J. 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 30
    • 0003512156 scopus 로고
    • (Cohn, E. J., and Edsall, J. T., Eds.), Reinhold Publishing Corp., New York
    • Cohn, E. J., and Edsall, J. T. (1943) in Proteins (Cohn, E. J., and Edsall, J. T., Eds.) pp 370-381, Reinhold Publishing Corp., New York.
    • (1943) Proteins , pp. 370-381
    • Cohn, E.J.1    Edsall, J.T.2
  • 31
    • 0021773239 scopus 로고
    • Hydrodynamic properties of bovine brain S-100 proteins
    • Mani, R. S., and Kay, C. M. (1984) Hydrodynamic properties of bovine brain S-100 proteins, FEBS Lett. 166, 258-262.
    • (1984) FEBS Lett. , vol.166 , pp. 258-262
    • Mani, R.S.1    Kay, C.M.2
  • 32
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • Kuntz, I. D., Jr., and Kauzmann, W. (1974) Hydration of proteins and polypeptides, Adv. Protein Chem. 28, 239-345.
    • (1974) Adv. Protein Chem. , vol.28 , pp. 239-345
    • Kuntz Jr., I.D.1    Kauzmann, W.2
  • 33
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A., and Johnson, W. C., Jr. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication, Anal. Biochem. 155, 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 34
    • 0035197209 scopus 로고    scopus 로고
    • Human XPA and XRCC1 DNA repair proteins expressed in yeast, Saccharomyces cerevisiae
    • Pushnova, E. A., Ostanin, K., and Thelen, M. P. (2001) Human XPA and XRCC1 DNA repair proteins expressed in yeast, Saccharomyces cerevisiae, Mol. Genet. Metab. 74, 380-384.
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 380-384
    • Pushnova, E.A.1    Ostanin, K.2    Thelen, M.P.3
  • 36
    • 0015239186 scopus 로고
    • Molecular sieve studies of interacting protein systems. VI. Effects of axial dispersion on boundary profiles of associating macromolecules
    • Zimmerman, J. K., and Ackers, G. K. (1971) Molecular sieve studies of interacting protein systems. VI. Effects of axial dispersion on boundary profiles of associating macromolecules, J. Biol. Chem. 246, 1078-1087.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1078-1087
    • Zimmerman, J.K.1    Ackers, G.K.2
  • 37
    • 0015218061 scopus 로고
    • Molecular sieve studies of interacting protein systems. IX. Reaction boundary profiles for monomer-n-mer systems: Comparison with sedimentation
    • Zimmerman, J. K., Cox, D. J., and Ackers, G. K. (1971) Molecular sieve studies of interacting protein systems. IX. Reaction boundary profiles for monomer-n-mer systems: comparison with sedimentation, J. Biol. Chem. 246, 4242-4250.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4242-4250
    • Zimmerman, J.K.1    Cox, D.J.2    Ackers, G.K.3
  • 38
    • 0019878623 scopus 로고
    • Self-association of rabbit muscle phosphofructokinase at pH 7.0: Stoichiometry
    • Hesterberg, L. K., and Lee, J. C. (1981) Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry, Biochemistry 20, 2974-2980.
    • (1981) Biochemistry , vol.20 , pp. 2974-2980
    • Hesterberg, L.K.1    Lee, J.C.2
  • 39
    • 0025845307 scopus 로고
    • Oligomeric protein associations: Transition from stochastic to deterministic equilibrium
    • Erijman, L., and Weber, G. (1991) Oligomeric protein associations: transition from stochastic to deterministic equilibrium, Biochemistry 30, 1595-1599.
    • (1991) Biochemistry , vol.30 , pp. 1595-1599
    • Erijman, L.1    Weber, G.2
  • 42
    • 0003605587 scopus 로고
    • Prentice-Hall, Englewood Cliffs, NJ
    • Van Holde, K. E. (1985) Physical Biochemistry, p 60, Prentice-Hall, Englewood Cliffs, NJ.
    • (1985) Physical Biochemistry , pp. 60
    • Van Holde, K.E.1
  • 43
    • 0023920362 scopus 로고
    • Pig heart calpastatin: Identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis
    • Takano, E., Maki, M., Mori, H., Hatanaka, M., Marti, T., Titani, K., Kannagi, R., Ooi, T., and Murachi, T. (1988) Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis, Biochemistry 27, 1964-1972.
    • (1988) Biochemistry , vol.27 , pp. 1964-1972
    • Takano, E.1    Maki, M.2    Mori, H.3    Hatanaka, M.4    Marti, T.5    Titani, K.6    Kannagi, R.7    Ooi, T.8    Murachi, T.9
  • 44
    • 11144258127 scopus 로고
    • Isolation and characterization of messenger-RNA from mammary-gland of lactating cow
    • Yoshikawa, M., Mizukami, T., Omori, K., Sasaki, R., and Chiba, H. (1981) Isolation and characterization of messenger-RNA from mammary-gland of lactating cow, Agric. Biol. Chem. 45, 177-183.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 177-183
    • Yoshikawa, M.1    Mizukami, T.2    Omori, K.3    Sasaki, R.4    Chiba, H.5
  • 46
    • 0242285628 scopus 로고    scopus 로고
    • Cell signaling. The BRCT domain: Signaling with friends?
    • Caldecott, K. W. (2003) Cell signaling. The BRCT domain: signaling with friends?, Science 302, 579-580.
    • (2003) Science , vol.302 , pp. 579-580
    • Caldecott, K.W.1
  • 47
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke, I. A., Lowery, D. M., Nguyen, A., and Yaffe, M. B. (2003) BRCT repeats as phosphopeptide-binding modules involved in protein targeting, Science 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
  • 48
    • 0034809456 scopus 로고    scopus 로고
    • Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1
    • Williams, R. S., Green, R., and Glover, J. N. (2001) Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1, Nat. Struct. Biol. 8, 838-842.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 838-842
    • Williams, R.S.1    Green, R.2    Glover, J.N.3
  • 51
    • 0037125135 scopus 로고    scopus 로고
    • Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly(ADP-ribose) polymerase-1 deficient murine cell extracts
    • Sanderson, R. J., and Lindahl, T. (2002) Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly(ADP-ribose) polymerase-1 deficient murine cell extracts, DNA Repair (Amsterdam) 1, 547-558.
    • (2002) DNA Repair (Amsterdam) , vol.1 , pp. 547-558
    • Sanderson, R.J.1    Lindahl, T.2
  • 52
    • 0014199062 scopus 로고
    • The binding of oligosaccharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme. The specificity of binding subsites
    • Chipman, D. M., Grisaro, V., and Sharon, N. (1967) The binding of oligosaccharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme. The specificity of binding subsites, J. Biol. Chem. 242, 4388-4394.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4388-4394
    • Chipman, D.M.1    Grisaro, V.2    Sharon, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.