Table of Contents Author Guidelines Submit a Manuscript
Journal of Nucleic Acids
Volume 2010, Article ID 304035, 11 pages
http://dx.doi.org/10.4061/2010/304035
Research Article

Targeting the OB-Folds of Replication Protein A with Small Molecules

1Department of Medicine/Hematology and Oncology, Indiana University School of Medicine, Joseph E. Walther Hall, R3-C562, 980 W. Walnut Street, Indianapolis, IN 46202, USA
2Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Joseph E. Walther Hall, R3-C562, 980 W. Walnut Street, Indianapolis, IN 46202, USA
3Department of Biochemistry, Vanderbilt University School of Medicine, 850 Robinson Research Building, Nashville, TN 37209, USA
4Department of Chemistry and Physics, Indiana State University, Terre Haute, IN 47809, USA

Received 19 August 2010; Accepted 27 September 2010

Academic Editor: Ashis Basu

Copyright © 2010 Victor J. Anciano Granadillo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. S. Wold, “Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism,” Annual Review of Biochemistry, vol. 66, pp. 61–92, 1997. View at Publisher · View at Google Scholar
  2. A. Bochkarev and E. Bochkareva, “From RPA to BRCA2: lessons from single-stranded DNA binding by the OB-fold,” Current Opinion in Structural Biology, vol. 14, no. 1, pp. 36–42, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. D. L. Theobald, R. M. Mitton-Fry, and D. S. Wuttke, “Nucleic acid recognition by OB-fold proteins,” Annual Review of Biophysics and Biomolecular Structure, vol. 32, pp. 115–133, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. M. Lei, E. R. Podell, and T. R. Cech, “Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection,” Nature Structural & Molecular Biology, vol. 11, no. 12, pp. 1223–1229, 2004. View at Google Scholar · View at Scopus
  5. F. Wang, E. R. Podell, A. J. Zaug et al., “The POT1-TPP1 telomere complex is a telomerase processivity factor,” Nature, vol. 445, no. 7127, pp. 506–510, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. H. Yang, P. D. Jeffrey, J. Miller et al., “BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure,” Science, vol. 297, no. 5588, pp. 1837–1848, 2002. View at Publisher · View at Google Scholar · View at Scopus
  7. A. G. Murzin, “OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences,” EMBO Journal, vol. 12, pp. 861–867, 1993. View at Google Scholar
  8. E. Bochkareva, S. Korolev, S. P. Lees-Miller, and A. Bochkarev, “Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA,” EMBO Journal, vol. 21, no. 7, pp. 1855–1863, 2002. View at Publisher · View at Google Scholar · View at Scopus
  9. R. A. Pfuetzner, A. Bochkarev, L. Frappier, and A. M. Edwards, “Replication protein A: characterization and crystallization of the DNA binding domain,” Journal of Biological Chemistry, vol. 272, no. 1, pp. 430–434, 1997. View at Publisher · View at Google Scholar · View at Scopus
  10. K. Umezu, N. Sugawara, C. Chen, J. E. Haber, and R. D. Kolodner, “Genetic analysis of yeast RPA1 reveals its multiple functions in DNA metabolism,” Genetics, vol. 148, no. 3, pp. 989–1005, 1998. View at Google Scholar · View at Scopus
  11. S. J. Haring, A. C. Mason, S. K. Binz, and M. S. Wold, “Cellular functions of human RPA1: multiple roles of domains in replication, repair, and checkpoints,” Journal of Biological Chemistry, vol. 283, no. 27, pp. 19095–19111, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. S. C. Shuck and J. J. Turchi, “Targeted inhibition of Replication Protein A reveals cytotoxic activity, synergy with chemotherapeutic DNA-damaging agents, and insight into cellular function,” Cancer Research, vol. 70, no. 8, pp. 3189–3198, 2010. View at Publisher · View at Google Scholar
  13. S. Waga and B. Stillman, “The DNA replication fork in eukaryotic cells,” Annual Review of Biochemistry, vol. 67, pp. 721–751, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. I. de Vlaminck, I. Vidic, M. T. J. van Loenhout, R. Kanaar, J. H. G. Lebbink, and C. Dekker, “Torsional regulation of hRPA-induced unwinding of double-stranded DNA,” Nucleic Acids Research, vol. 38, no. 12, pp. 4133–4142, 2010. View at Publisher · View at Google Scholar
  15. D. B. Zamble, D. Mu, J. T. Reardon, A. Sancar, and S. J. Lippard, “Repair of cisplatin-DNA adducts by the mammalian excision nuclease,” Biochemistry, vol. 35, no. 31, pp. 10004–10013, 1996. View at Publisher · View at Google Scholar · View at Scopus
  16. S. M. Patrick and J. J. Turchi, “Xeroderma pigmentosum complementation group A protein (XPA) modulates RPA-DNA interactions via enhanced complex stability and inhibition of strand separation activity,” Journal of Biological Chemistry, vol. 277, no. 18, pp. 16096–16101, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. S. M. Patrick and J. J. Turchi, “Replication protein a (RPA) binding to duplex cisplatin-damaged DNA is mediated through the generation of single-stranded DNA,” Journal of Biological Chemistry, vol. 274, no. 21, pp. 14972–14978, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. S. M. Patrick, K. Tillison, and J. M. Horn, “Recognition of cisplatin-DNA interstrand cross-links by replication protein A,” Biochemistry, vol. 47, no. 38, pp. 10188–10196, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. E. Reed, “Platinum-DNA adduct, nucleotide excision repair and platinum based anti-cancer chemotherapy,” Cancer Treatment Reviews, vol. 24, no. 5, pp. 331–344, 1998. View at Google Scholar
  20. M. E. Stauffer and W. J. Chazin, “Physical interaction between replication protein A and Rad51 promootes exchange on single-stranded DNA,” Journal of Biological Chemistry, vol. 279, no. 24, pp. 25638–25645, 2004. View at Publisher · View at Google Scholar · View at Scopus
  21. C. Soustelle, M. Vedel, R. Kolodner, and A. Nicolas, “Replication protein A is required for meiotic recombination in Saccharomyces cerevisiae,” Genetics, vol. 161, no. 2, pp. 535–547, 2002. View at Google Scholar · View at Scopus
  22. J. J. Turchi, S. C. Shuck, E. A. Short, and B. J. Andrews, “Targeting nucleotide excision repair as a mechanism to increase cisplatin efficacy,” in Platinum and Other Heavy Metal Compounds in Cancer Chemotherapy, A. Bonetti, R. Leone, F. M. Muggia, and S. B. Howell, Eds., Humana Press, New York, NY, USA, 2009. View at Google Scholar
  23. B. J. Andrews, J. A. Lehman, and J. J. Turchi, “Kinetic analysis of the Ku-DNA binding activity reveals a redox-dependent alteration in protein structure that stimulates dissociation of the Ku-DNA complex,” Journal of Biological Chemistry, vol. 281, no. 19, pp. 13596–13603, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. B. J. Andrews and J. J. Turchi, “Development of a high-throughput screen for inhibitors of replication protein A and its role in nucleotide excision repair,” Molecular Cancer Therapeutics, vol. 3, no. 4, pp. 385–391, 2004. View at Google Scholar · View at Scopus
  25. I. M. Wyka, K. Dhar, S. K. Binz, and M. S. Wold, “Replication Protein A interactions with DNA: differential binding of the core domains and analysis of the DNA interaction surface,” Biochemistry, vol. 42, no. 44, pp. 12909–12918, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. E. Bochkareva, V. Belegu, S. Korolev, and A. Bochkarev, “Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding,” EMBO Journal, vol. 20, no. 3, pp. 612–618, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Bochkarev, R. A. Pfuetzner, A. M. Edwards, and L. Frappier, “Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA,” Nature, vol. 385, no. 6612, pp. 176–181, 1997. View at Publisher · View at Google Scholar · View at Scopus
  28. R. I. Murray, I. C. Gunsalus, and K. M. Dus, “Active site studies of cytochrome P=450CAM. I. Specific cysteine labeling with the affinity reagent isobornyl bromoacetate as a model for substrate binding,” Journal of Biological Chemistry, vol. 257, no. 21, pp. 12517–12525, 1982. View at Google Scholar · View at Scopus
  29. M. Lei, E. R. Podell, P. Baumann, and T. R. Cech, “DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA,” Nature, vol. 426, no. 6963, pp. 198–202, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. J. E. Croy, E. R. Podell, and D. S. Wuttke, “A new model for schizosaccharomyces pombe telomere recognition: the telomeric single-stranded DNA-binding Activity of Pot11-389,” Journal of Molecular Biology, vol. 361, no. 1, pp. 80–93, 2006. View at Publisher · View at Google Scholar · View at Scopus
  31. S. Raghunathan, A. G. Kozlov, T. M. Lohman, and G. Waksman, “Structure of the heterodimeric complex between CAD domains of CAD and ICAD,” Nature Structural Biology, vol. 7, no. 8, pp. 658–662, 2000. View at Publisher · View at Google Scholar · View at Scopus
  32. P. Y. Ng, Y. Tang, W. M. Knosp, H. S. Stadler, and J. T. Shaw, “Synthesis of diverse lactam carboxamides leading to the discovery of a new transcription-factor inhibitor,” Angewandte Chemie, vol. 46, no. 28, pp. 5352–5355, 2007. View at Publisher · View at Google Scholar · View at Scopus
  33. R. E. Moellering, M. Cornejo, T. N. Davis et al., “Direct inhibition of the NOTCH transcription factor complex,” Nature, vol. 462, no. 7270, pp. 182–188, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. M. N. Saha, H. Jiang, J. Jayakar, D. Reece, D. R. Branch, and H. Chang, “MDM2 antagonist nutlin plus proteasome inhibitor velcade combination displays a synergistic anti-myeloma activity,” Cancer Biology and Therapy, vol. 9, no. 11, pp. 937–945, 2010. View at Google Scholar