Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
권호 표지
DOI QR코드

DOI QR Code

Solution Structure of LXXLL-related Cofactor Peptide of Orphan Nuclear Receptor FTZ-F1

  • Yun, Ji-Hye (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University) ;
  • Lee, Chul-Jin (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University) ;
  • Jung, Jin-Won (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University) ;
  • Lee, Weon-Tae (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University)
  • Received : 2011.11.09
  • Accepted : 2011.12.15
  • Published : 2012.02.20
Download PDF
⟨ Previous Next ⟩

Abstract

Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide ($FTZ^{PEP}$) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, $FTZ^{PEP}$ formed ${\alpha}$-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of $FTZ^{PEP}$. The solution structure of $FTZ^{PEP}$ in the presence of FTZ-F1 displays a long stretch of the ${\alpha}$-helix with a bend in the middle of helix.

Keywords

References

  1. Guichet, A.; Copeland, J. W.; Erdelyi, M.; Hlousek, D.; Zavorszky, P.; Ho, J.; Brown, S.; Percival-Smith, A.; Krause, H. M.; Ephrussi, A. Nature 1997, 385(6616), 548-552. https://doi.org/10.1038/385548a0
  2. Yu, Y.; Li, W.; Su, K.; Yussa, M.; Han, W.; Perrimon, N.; Pick, L. Nature 1997, 385(6616), 552-555. https://doi.org/10.1038/385552a0
  3. Yoo, J.; Ko, S.; Kim, H.; Sampson, H.; Yun, J.-H.; Choe, K.-M.; Chang, I. S.; Lee, W. J. Biol. Chem. 2011, 286(36), 31225-31231. https://doi.org/10.1074/jbc.M111.252916
  4. Kastner, P.; Mark, M.; Chambon, P. Cell 1995, 83(6), 859-869. https://doi.org/10.1016/0092-8674(95)90202-3
  5. Mangelsdorf, D. J.; Evans, R. M. Cell 1995, 83(6), 841-850. https://doi.org/10.1016/0092-8674(95)90200-7
  6. Mangelsdorf, D. J.; Thummel, C.; Beato, M.; Herrlich, P.; Schutz, G.; Umesono, K.; Blumberg, B.; Kastner, P.; Mark, M.; Chambon, P.; Evans, R. M. Cell 1995, 83(6), 835-839. https://doi.org/10.1016/0092-8674(95)90199-X
  7. Thummel, C. S. Cell 1995, 83(6), 871-877. https://doi.org/10.1016/0092-8674(95)90203-1
  8. Blumberg, B.; Evans, R. M. Genes Dev. 1998, 12(20), 3149-3155. https://doi.org/10.1101/gad.12.20.3149
  9. Giguere, V. Endocr. Rev. 1999, 20(5), 689-725. https://doi.org/10.1210/er.20.5.689
  10. Bourguet, W.; Ruff, M.; Chambon, P.; Gronemeyer, H.; Moras, D. Nature 1995, 375(6530), 377-382. https://doi.org/10.1038/375377a0
  11. Renaud, J. P.; Rochel, N.; Ruff, M.; Vivat, V.; Chambon, P.; Gronemeyer, H.; Moras, D. Nature 1995, 378(6558), 681-689. https://doi.org/10.1038/378681a0
  12. Brzozowski, A. M.; Pike, A. C.; Dauter, Z.; Hubbard, R. E.; Bonn, T.; Engstrom, O.; Ohman, L.; Greene, G. L.; Gustafsson, J. A.; Carlquist, M. Nature 1997, 389(6652), 753-758. https://doi.org/10.1038/39645
  13. Shiau, A. K.; Barstad, D.; Loria, P. M.; Cheng, L.; Kushner, P. J.; Agard, D. A.; Greene, G. L. Cell 1998, 95(7), 927-937. https://doi.org/10.1016/S0092-8674(00)81717-1
  14. Sablin, E. P.; Krylova, I. N.; Fletterick, R. J.; Ingraham, H. A. Mol. Cell 2003, 11(6), 1575-1585. https://doi.org/10.1016/S1097-2765(03)00236-3
  15. Suzuki, T.; Kasahara, M.; Yoshioka, H.; Morohashi, K.; Umesono, K. Mol. Cell Biol. 2003, 23(1), 238-249. https://doi.org/10.1128/MCB.23.1.238-249.2003
  16. Ueda, H.; Sonoda, S.; Brown, J. L.; Scott, M. P.; Wu, C. Genes Dev. 1990, 4(4), 624-635. https://doi.org/10.1101/gad.4.4.624
  17. Carroll, S. B.; Scott, M. P. Cell 1985, 43(1), 47-57. https://doi.org/10.1016/0092-8674(85)90011-X
  18. Wakimoto, B. T.; Turner, F. R.; Kaufman, T. C. Dev. Biol. 1984, 102(1), 147-172. https://doi.org/10.1016/0012-1606(84)90182-9
  19. Desplan, C.; Theis, J.; O'Farrell, P. H. Cell 1988, 54(7), 1081-1090. https://doi.org/10.1016/0092-8674(88)90123-7
  20. Schwartz, C. J.; Sampson, H. M.; Hlousek, D.; Percival-Smith, A.; Copeland, J. W.; Simmonds, A. J.; Krause, H. M. Embo. J. 2001, 20(3), 510-519. https://doi.org/10.1093/emboj/20.3.510
  21. Feng, W.; Ribeiro, R. C.; Wagner, R. L.; Nguyen, H.; Apriletti, J. W.; Fletterick, R. J.; Baxter, J. D.; Kushner, P. J.; West, B. L. Science 1998, 280(5370), 1747-1749. https://doi.org/10.1126/science.280.5370.1747
  22. Mak, H. Y.; Hoare, S.; Henttu, P. M.; Parker, M. G. Mol. Cell Biol. 1999, 19(5), 3895-3903. https://doi.org/10.1128/MCB.19.5.3895
  23. Johansson, L.; Bavner, A.; Thomsen, J. S.; Farnegardh, M.; Gustafsson, J. A.; Treuter, E. Mol. Cell Biol. 2000, 20(4), 1124- 1133. https://doi.org/10.1128/MCB.20.4.1124-1133.2000
  24. Marion, D.; Wuthrich, K. Biochem. Biophys. Res. Commun. 1983, 113(3), 967-974. https://doi.org/10.1016/0006-291X(83)91093-8
  25. Rance, M.; Sorensen, O. W.; Bodenhausen, G.; Wagner, G.; Ernst, R. R.; Wuthrich, K. Biochem. Biophys. Res. Commun. 1983, 117(2), 479-485. https://doi.org/10.1016/0006-291X(83)91225-1
  26. Piotto, M.; Saudek, V.; Sklenar, V. J. Biomol. NMR 1992, 2(6), 661-665. https://doi.org/10.1007/BF02192855
  27. Driscoll, P. C.; Gronenborn, A. M.; Beress, L.; Clore, G. M. Biochemistry 1989, 28(5), 2188-2198. https://doi.org/10.1021/bi00431a033
  28. Wuthrich, K.; Billeter, M.; Braun, W. J. Mol. Biol. 1983, 169(4), 949-961. https://doi.org/10.1016/S0022-2836(83)80144-2

Cited by

  1. Folding Simulations of a Nuclear Receptor Box-Containing Peptide Demonstrate the Structural Persistence of the LxxLL Motif Even in the Absence of Its Cognate Receptor vol.122, pp.1, 2018, https://doi.org/10.1021/acs.jpcb.7b10292