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Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1

Nature Structural Biology volume 9, pages 247–251 (2002)Cite this article

Abstract

The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four α-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.

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Figure 1: Characterization of TapC and point mutants.
Figure 2: Solution structure of the Tap C-terminal domain.
Figure 3: Features of the Tap C-terminal domain.
Figure 4: Interaction between TapC and FG-nucleoporins.

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References

  1. Cullen, B.R. Mol. Cell. Biol. 20, 4181–4187 (2000).

    Article  CAS  Google Scholar 

  2. Ryan, K.J. & Wente, S. Curr. Opin. Cell Biol. 12, 361–371 (2001).

    Article  Google Scholar 

  3. Stewart, M. et al. FEBS Lett. 498, 145–149 (2001).

    Article  CAS  Google Scholar 

  4. Damelin, M. & Silver, P.A. Mol. Cell 5, 133–140 (2000).

    Article  CAS  Google Scholar 

  5. Rout, M.P. et al. J. Cell Biol. 148, 635–652 (2000).

    Article  CAS  Google Scholar 

  6. Ribbeck, K. & Görlich, D. EMBO J. 20, 1320–1330 (2001).

    Article  CAS  Google Scholar 

  7. Segref, A. et al. EMBO J. 16, 3256–3271 (1997).

    Article  CAS  Google Scholar 

  8. Herold, A. et al. Mol. Cell. Biol. 20, 8996–9008 (2000).

    Article  CAS  Google Scholar 

  9. Tan, W., Zolotukhin, A.S., Bear, J., Patenaude, D.J. & Feldber, B.K. RNA 6, 1762–1772 (2000).

    Article  CAS  Google Scholar 

  10. Braun, I.C., Herold, A., Rode, M., Conti, E. & Izaurralde, E. J. Biol. Chem. 276, 20536–20543 (2001).

    Article  CAS  Google Scholar 

  11. Strässer, K., Bassler, J. & Hurt, E. J. Cell Biol. 150, 695–706 (2000).

    Article  Google Scholar 

  12. Weingand, H.L. et al. Mol. Cell. Biol. 22, 245–256 (2002).

    Article  Google Scholar 

  13. Levesque, L. et al. J. Biol. Chem. 276, 44953–44962 (2001).

    Article  CAS  Google Scholar 

  14. Katahira, J. et al. EMBO J. 18, 2593–2609 (1999).

    Article  CAS  Google Scholar 

  15. Kang, Y. & Cullen, B.R. Genes Dev. 13, 1126–1139 (1999).

    Article  CAS  Google Scholar 

  16. Liker, E., Fernandez, E., Izaurralde, E. & Conti, E. EMBO J. 19, 5587–5598 (2000).

    Article  CAS  Google Scholar 

  17. Fribourg, S., Braun, I.C., Izaurralde, E. & Conti, E. Mol. Cell 8, 645–656 (2001).

    Article  CAS  Google Scholar 

  18. Schmitt, I. & Gerace, L. J. Biol. Chem. 276, 42355–42363 (2001).

    Article  CAS  Google Scholar 

  19. Bachi, A. et al. RNA 6, 136–158 (2000).

    Article  CAS  Google Scholar 

  20. Kang, Y., Bogerd, H.P. & Cullen, B.R. J. Virol. 74, 5863–5871 (2000).

    Article  CAS  Google Scholar 

  21. Suyama, M. et al. EMBO Rep. 1, 53–58 (2000).

    Article  CAS  Google Scholar 

  22. Clarkson, W.D., Kent, H.M. & Stewart, M. J. Mol. Biol. 263, 517–524 (1996).

    Article  CAS  Google Scholar 

  23. Withers-Ward, E.S. et al. Biochemistry 39, 14103–14112 (2000).

    Article  CAS  Google Scholar 

  24. Bayliss, R. et al. J. Mol. Biol. 293, 579–593 (1999).

    Article  CAS  Google Scholar 

  25. Bayliss, R., Littlewood, T.D. & Stewart, M. Cell 102, 99–108 (2000).

    Article  CAS  Google Scholar 

  26. Wüthrich, K. NMR of proteins and nucleic acids (John Wiley, New York; 1986).

    Book  Google Scholar 

  27. Hommel, U., Harvey, T.S., Driscoll, P.C. & Campbell, I.D. J. Mol. Biol. 227, 271–282 (1992).

    Article  CAS  Google Scholar 

  28. Nilges, M. J. Mol. Biol. 245, 645–660 (1995).

    Article  CAS  Google Scholar 

  29. Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. Protein Eng. 2, 27–38 (1988).

    Article  CAS  Google Scholar 

  30. Brünger, A.T. X-PLOR Version 3.1(Yale University, New Haven; 1992).

    Google Scholar 

  31. Diamond, R. Acta Crystallogr. D 51, 127–135 (1995).

    Article  CAS  Google Scholar 

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Acknowledgements

We are grateful to our colleagues in Cambridge and Heidelberg, especially R. Bayliss, T. Littlewood, K. Strässer and A. Weeds for their helpful comments and criticisms. We thank J.C. Yang for help in recording NMR spectra, S. Peak-Chew for N-terminal sequencing and mass spectroscopy, and G. Wong for preparing proteins. Supported in part by the Human Frontiers Science Program.

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Richard P. Grant, David Neuhaus & Murray Stewart

  2. Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, Heidelberg, 69120, Germany

    Ed Hurt

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  1. Richard P. Grant
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Correspondence to Murray Stewart.

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Grant, R., Hurt, E., Neuhaus, D. et al. Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. Nat Struct Mol Biol 9, 247–251 (2002). https://doi.org/10.1038/nsb773

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