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BioMed Research International
Volume 2014 (2014), Article ID 285791, 8 pages
http://dx.doi.org/10.1155/2014/285791
Research Article

The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster

Department of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, LA 70803, USA

Received 9 June 2014; Accepted 8 July 2014; Published 24 July 2014

Academic Editor: Cheng-Yang Huang

Copyright © 2014 Aaron P. Landry and Huangen Ding. 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. T. de Lange, “How telomeres solve the end-protection problem,” Science, vol. 326, no. 5955, pp. 948–952, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. A. Sfeir, S. T. Kosiyatrakul, D. Hockemeyer et al., “Mammalian telomeres resemble fragile sites and require TRF1 for efficient replication,” Cell, vol. 138, no. 1, pp. 90–103, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. E. H. Blackburn, “Switching and signaling at the telomere,” Cell, vol. 106, no. 6, pp. 661–673, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. H. Ding, M. Schertzer, X. Wu et al., “Regulation of murine telomere length by Rtel: an essential gene encoding a helicase-like protein,” Cell, vol. 117, no. 7, pp. 873–886, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. Y. Jeffrey Chiang, R. T. Calado, K. S. Hathcock, P. M. Lansdorp, N. S. Young, and R. J. Hodes, “Telomere length is inherited with resetting of the telomere set-point,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 22, pp. 10148–10153, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. E. Uringa, J. L. Youds, K. Lisaingo, P. M. Lansdorp, and S. J. Boulton, “RTEL1: an essential helicase for telomere maintenance and the regulation of homologous recombination,” Nucleic Acids Research, vol. 39, no. 5, pp. 1647–1655, 2011. View at Publisher · View at Google Scholar · View at Scopus
  7. C. Bai, B. Connolly, M. L. Metzker et al., “Overexpression of M68/DcR3 in human gastrointestinal tract tumors independent of gene amplification and its location in a four-gene cluster,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 3, pp. 1230–1235, 2000. View at Publisher · View at Google Scholar · View at Scopus
  8. A. J. Walne, T. Vulliamy, M. Kirwan, V. Plagnol, and I. Dokal, “Constitutional mutations in RTEL1 cause severe dyskeratosis congenita,” The American Journal of Human Genetics, vol. 92, no. 3, pp. 448–453, 2013. View at Publisher · View at Google Scholar · View at Scopus
  9. B. J. Ballew, M. Yeager, K. Jacobs et al., “Germline mutations of regulator of telomere elongation helicase 1, RTEL1, in Dyskeratosis congenita,” Human Genetics, vol. 132, no. 4, pp. 473–480, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. M. E. Fairman-Williams, U. P. Guenther, and E. Jankowsky, “SF1 and SF2 helicases: family matters,” Current Opinion in Structural Biology, vol. 20, no. 3, pp. 313–324, 2010. View at Publisher · View at Google Scholar · View at Scopus
  11. M. F. White, “Structure, function and evolution of the XPD family of iron-sulfur-containing 5′→3′ DNA helicases,” Biochemical Society Transactions, vol. 37, no. 3, pp. 547–551, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. S. B. Cantor and S. Guillemette, “Hereditary breast cancer and the BRCA1-associated FANCJ/BACH1/BRIP1,” Future Oncology, vol. 7, no. 2, pp. 253–261, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. J. A. Sommers, N. Rawtani, R. Gupta et al., “FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange,” The Journal of Biological Chemistry, vol. 284, no. 12, pp. 7505–7517, 2009. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Wu, J. A. Sommers, I. Khan, J. P. de Winter, and R. M. Brosh Jr., “Biochemical characterization of Warsaw breakage syndrome helicase,” Journal of Biological Chemistry, vol. 287, no. 2, pp. 1007–1021, 2012. View at Publisher · View at Google Scholar · View at Scopus
  15. J. L. Youds, D. G. Mets, M. J. McIlwraith et al., “RTEL-1 enforces meiotic crossover interference and homeostasis,” Science, vol. 327, no. 5970, pp. 1254–1258, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. L. J. Barber, J. L. Youds, J. D. Ward et al., “RTEL1 maintains genomic stability by suppressing homologous recombination,” Cell, vol. 135, no. 2, pp. 261–271, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. M. F. White and M. S. Dillingham, “Iron-sulphur clusters in nucleic acid processing enzymes,” Current Opinion in Structural Biology, vol. 22, no. 1, pp. 94–100, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. R. A. Pugh, M. Honda, H. Leesley et al., “The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction,” The Journal of Biological Chemistry, vol. 283, no. 3, pp. 1732–1743, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. H. Liu, J. Rudolf, K. A. Johnson et al., “Structure of the DNA Repair Helicase XPD,” Cell, vol. 133, no. 5, pp. 801–812, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. L. Fan, J. O. Fuss, Q. J. Cheng et al., “XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations,” Cell, vol. 133, no. 5, pp. 789–800, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. S. C. Wolski, J. Kuper, P. Hänzelmann et al., “Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD,” PLoS Biology, vol. 6, article e149, no. 6, 2008. View at Publisher · View at Google Scholar · View at Scopus
  22. J. Rudolf, V. Makrantoni, W. J. Ingledew, M. J. R. Stark, and M. F. White, “The DNA repair helicases XPD and FancJ have essential iron-sulfur domains,” Molecular Cell, vol. 23, no. 6, pp. 801–808, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. B. Ren, X. Duan, and H. Ding, “Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster,” Journal of Biological Chemistry, vol. 284, no. 8, pp. 4829–4835, 2009. View at Publisher · View at Google Scholar · View at Scopus
  24. J. T. P. Yeeles, R. Cammack, and M. S. Dillingham, “An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases,” The Journal of Biological Chemistry, vol. 284, no. 12, pp. 7746–7755, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. R. E. Cowart, F. L. Singleton, and J. S. Hind, “A comparison of bathophenanthrolinedisulfonic acid and ferrozine as chelators of iron(II) in reduction reactions,” Analytical Biochemistry, vol. 211, no. 1, pp. 151–155, 1993. View at Publisher · View at Google Scholar · View at Scopus
  26. L. M. Siegel, “A direct microdetermination for sulfide,” Analytical Biochemistry, vol. 11, no. 1, pp. 126–132, 1965. View at Publisher · View at Google Scholar · View at Scopus
  27. R. D. Shereda, A. G. Kozlov, T. M. Lohman, M. M. Cox, and J. L. Keck, “SSB as an organizer/mobilizer of genome maintenance complexes,” Critical Reviews in Biochemistry and Molecular Biology, vol. 43, no. 5, pp. 289–318, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. Z. Cheng, A. Caillet, B. Ren, and H. Ding, “Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB,” FEBS Letters, vol. 586, no. 21, pp. 3825–3830, 2012. View at Publisher · View at Google Scholar · View at Scopus
  29. P. Leslie Dutton, “Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems,” Methods in Enzymology, vol. 54, pp. 411–435, 1978. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Böhm, R. Muhr, and R. Jaenicke, “Quantitative analysis of protein far UV circular dichroism spectra by neural networks,” Protein Engineering, vol. 5, no. 3, pp. 191–195, 1992. View at Google Scholar · View at Scopus
  31. K. Müller, B. F. Matzanke, V. Schünemann, A. X. Trautwein, and K. Hantke, “FhuF, an iron-regulated protein of Escherichia coli with a new type of [2Fe-2S] center,” European Journal of Biochemistry, vol. 258, no. 3, pp. 1001–1008, 1998. View at Publisher · View at Google Scholar · View at Scopus
  32. S. Jang and J. A. Imlay, “Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes,” The Journal of Biological Chemistry, vol. 282, no. 2, pp. 929–937, 2007. View at Publisher · View at Google Scholar · View at Scopus
  33. A. P. Landry, X. Duan, H. Huang, and H. Ding, “Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress,” Free Radical Biology and Medicine, vol. 50, no. 11, pp. 1582–1590, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. D. R. Hyduke, L. R. Jarboe, L. M. Tran, K. J. Y. Chou, and J. C. Liao, “Integrated network analysis identifies nitric oxide response networks and dihydroxyacid dehydratase as a crucial target in Escherichia coli,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 20, pp. 8484–8489, 2007. View at Publisher · View at Google Scholar · View at Scopus
  35. Y. Wu and R. M. Brosh Jr., “DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster,” Nucleic Acids Research, vol. 40, no. 10, pp. 4247–4260, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. C. T. Dooley, T. M. Dore, G. T. Hanson, W. C. Jackson, S. J. Remington, and R. Y. Tsien, “Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators,” Journal of Biological Chemistry, vol. 279, no. 21, pp. 22284–22293, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. J. M. Hansen, Y. M. Go, and D. P. Jones, “Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling,” Annual Review of Pharmacology and Toxicology, vol. 46, pp. 215–234, 2006. View at Publisher · View at Google Scholar · View at Scopus
  38. J. M. J. Houben, H. J. J. Moonen, F. J. van Schooten, and G. J. Hageman, “Telomere length assessment: biomarker of chronic oxidative stress?” Free Radical Biology and Medicine, vol. 44, no. 3, pp. 235–246, 2008. View at Publisher · View at Google Scholar · View at Scopus