XRCC1 interaction with the REV1 C-terminal domain suggests a role in post replication repair

DNA Repair

Volumn 12, Issue 12, 2013, Pages 1105-1113

  Gabel, Scott A ^a   DeRose, Eugene F ^a   London, Robert E ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

NMR spectroscopy; Post replication repair; REV1 C terminal domain; REV1 interacting region; XRCC1

Indexed keywords

DNA POLYMERASE REV1; LIGAND; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; XRCC1 PROTEIN;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISSOCIATION CONSTANT; DNA REPAIR; DNA REPLICATION; ESCHERICHIA COLI; EXCISION REPAIR; FLUORESCENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE ANALYSIS; TITRIMETRY;

RUMEX;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; DNA DAMAGE; DNA REPAIR; DNA REPLICATION; DNA-BINDING PROTEINS; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR PROTEINS; NUCLEOTIDYLTRANSFERASES; POLYMORPHISM, GENETIC; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84888128365     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2013.08.015     Document Type: Article

References (53)

1. Caldecott K.W. XRCC1 and DNA strand break repair. DNA Repair 2003, 2(9):955-969.
2. Luo H., et al. A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment. Molecular and Cellular Biology 2004, 24(19):8356-8365.
3. Cappelli E., et al. Involvement of XRCC1 and DNA ligase III gene products in DNA base excision repair. Journal of Biological Chemistry 1997, 272(38):23970-23975.
4. Kubota Y., et al. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO Journal 1996, 15(23):6662-6670.
5. Masson M., et al. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Molecular and Cellular Biology 1998, 18(6):3563-3571.
6. Loeffler P.A., et al. Structural studies of the PARP-1 BRCT domain. BMC Structural Biology 2011, 11:37.
7. Okano S., et al. Spatial and temporal cellular responses to single-strand breaks in human cells. Molecular and Cellular Biology 2003, 23(11):3974-3981.
8. Fan J.S., et al. XRCC1 co-localizes and physically interacts with PCNA. Nucleic Acids Research 2004, 32(7):2193-2201.
9. Kiriyama T., et al. Restoration of nuclear-import failure caused by triple A syndrome and oxidative stress. Biochemical and Biophysical Research Communications 2008, 374(4):631-634.
10. Moser J., et al. Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III alpha in a cell-cycle-specific manner. Molecular Cell 2007, 27(2):311-323.
11. Ogi T., et al. Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells. Molecular Cell 2010, 37(5):714-727.
12. Whitehouse C.J., et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 2001, 104(1):107-117.
13. Ali A.A.E., et al. Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. Nucleic Acids Research 2009, 37(5):1701-1712.
14. Iles N., et al. APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Molecular and Cellular Biology 2007, 27(10):3793-3803.
15. Caldecott K.W., et al. An interaction between the Mammalian DNA-repair protein Xrcc1 and DNA ligase-III. Molecular and Cellular Biology 1994, 14(1):68-76.
16. Cuneo M.J., et al. The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes. Nucleic Acids Research 2011, 39(17):7816-7827.
17. Tissier A., et al. Co-localization in replication foci and interaction of human Y-family members. DNA polymerase pol eta and REV1 protein. DNA Repair 2004, 3(11):1503-1514.
18. D'souza S., Waters L.S., Walker G.C. Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance. DNA Repair 2008, 7(9):1455-1470.
19. Ohashi E., et al. Identification of a novel REV1-interacting motif necessary for DNA polymerase kappa function. Genes to Cells 2009, 14(2):101-111.
20. Hanssen-Bauer A., et al. The region of XRCC1 which harbours the three most common nonsynonymous polymorphic variants, is essential for the scaffolding function of XRCC1. DNA Repair 2012, 11(4):357-366.
21. Goode E.L., Ulrich C.M., Potter J.D. Polymorphisms in DNA repair genes and associations with cancer risk. Cancer Epidemiology Biomarkers and Prevention 2002, 11(12):1513-1530.
22. Zienolddiny S., et al. Polymorphisms of DNA repair genes and risk of non-small cell lung cancer. Carcinogenesis 2006, 27(3):560-567.
23. Chiyomaru K., Nagano T., Nishigori C. XRCC1 Arg194Trp polymorphism, risk of nonmelanoma skin cancer and extramammary Paget's disease in a Japanese population. Archives for Dermatological Research 2012, 304(5):363-370.
24. Huang M.S., et al. High-order interactions among genetic variants in DNA base excision repair pathway genes and smoking in bladder cancer susceptibility. Cancer Epidemiology Biomarkers and Prevention 2007, 16(1):84-91.
25. Moller M., Denicola A. Protein tryptophan accessibility studied by fluorescence quenching. Biochemistry and Molecular Biology Education 2002, 30(3):175-178.
26. Sulkowska A. Interaction of drugs with bovine and human serum albumin. Journal of Molecular Structure 2002, 614(1-3):227-232.
27. Delaglio F., et al. Nmrpipe - a multidimensional spectral processing system based on Unix pipes. Journal of Biomolecular NMR 1995, 6(3):277-293.
28. Johnson B.A., Blevins R.A. NMR view - a computer-program for the visualization and analysis of NMR data. Journal of Biomolecular NMR 1994, 4(5):603-614.
29. Sklenar V., et al. Gradient-tailored water suppression for H-1-N-15 Hsqc experiments optimized to retain full sensitivity. Journal of Magnetic Resonance Series A 1993, 102(2):241-245.
30. Zwahlen C., et al. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA complex. Journal of the American Chemical Society 1997, 119(29):6711-6721.
31. Pozhidaeva A., et al. NMR structure and dynamics of the C-terminal domain from human Revl and its complex with Rev1 interacting region of DNA polymerase eta. Biochemistry 2012, 51(27):5506-5520.
32. Wojtaszek J., et al. Multifaceted recognition of vertebrate Rev1 by Translesion polymerases zeta and kappa. Journal of Biological Chemistry 2012, 287(31):26400-26408.
33. 2O. Journal of Magnetic Resonance Series B 1994, 103(2):197-201.
34. Perlman M.E., et al. Studies of inhibitor binding to Escherichia coli purine nucleoside phosphorylase using the transferred nuclear Overhauser effect and rotating-frame nuclear Overhauser enhancement. Biochemistry 1994, 33(24):7547-7559.
35. Clore G.M. Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization. Proceedings of the National Academy of Sciences of the United States of America 2000, 97(16):9021-9025.
36. Wang G.S., et al. Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA (glucose) of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system. EMBO Journal 2000, 19(21):5635-5649.
37. Schwieters C.D., et al. The Xplor-NIH NMR molecular structure determination package. Journal of Magnetic Resonance 2003, 160(1):65-73.
38. Wojtaszek J., et al. Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa. Journal of Biological Chemistry 2012, 287(40):33836-33846.
39. Chou P.Y., Fasman G.D. Conformational parameters for amino-acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974, 13(2):211-222.
40. Malkov S.N., et al. A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure. Journal of Molecular Modeling 2008, 14(8):769-775.
41. Diamant N., et al. DNA damage bypass operates in the S and G2 phases of the cell cycle and exhibits differential mutagenicity. Nucleic Acids Research 2012, 40(1):170-180.
42. Sale J.E., Lehmann A.R., Woodgate R. Y-family DNA polymerases and their role in tolerance of cellular DNA damage. Nature Reviews Molecular Cell Biology 2012, 13(3):141-152.
43. Waters L.S., et al. Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance. Microbiology and Molecular Biology Reviews 2009, 73(1):134-154.
44. Kim H., et al. Regulation of Rev1 by the Fanconi anemia core complex. Nature Structural and Molecular Biology 2012, 19(2):164-170.
45. Bruning J.B., Shamoo Y. Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1. Structure 2004, 12(12):2209-2219.
46. Warbrick E. PCNA binding through a conserved motif. Bioessays 1998, 20(3):195-199.
47. De Biasio A., et al. Proliferating cell nuclear antigen (PCNA) interactions in solution studied by NMR. PLoS One 2012, 7(11):e48390.
48. Kubota Y., et al. Localization of X-ray cross complementing gene 1 protein in the nuclear matrix is controlled by casein kinase II-dependent phosphorylation in response to oxidative damage. DNA Repair 2009, 8(8):953-960.
49. Chou W.C., et al. Chk2-dependent phosphorylation of XRCC1 in the DNA damage response promotes base excision repair. EMBO Journal 2008, 27(23):3140-3150.
50. Loizou J.I., et al. The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks. Cell 2004, 117(1):17-28.
51. Molina H., et al. Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America 2007, 104(7):2199-2204.
52. Marqusee S., Baldwin R.L. Helix stabilization by Glu. Lys+ salt bridges in short peptides of Denovo design. Proceedings of the National Academy of Sciences of the United States of America 1987, 84(24):8898-8902.
53. Han J.L., et al. A prospective study of XRCC1 haplotypes and their interaction with plasma carotenoids on breast cancer risk. Cancer Research 2003, 63(23):8536-8541.