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NMR disentangles a dynamic disaggregase machinery

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The three-dimensional structure of a key complex in chaperone-mediated protein disaggregation, comprising ClpB and DnaK, has been determined using NMR. In addition to providing unique mechanistic insights, the approach promises to elucidate the structural basis for the assembly of elusive dynamic protein machineries in the near future.

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Figure 1: Chaperones and cofactors involved in the ClpB disaggregase machinery.

References

  1. Hartl, F.U., Bracher, A. & Hayer-Hartl, M. Nature 475, 324–332 (2011).

    Article  CAS  Google Scholar 

  2. Hartl, F.U. & Hayer-Hartl, M. Nat. Struct. Mol. Biol. 16, 574–581 (2009).

    Article  CAS  Google Scholar 

  3. Tyedmers, J., Mogk, A. & Bukau, B. Nat. Rev. Mol. Cell Biol. 11, 777–788 (2010).

    Article  CAS  Google Scholar 

  4. Doyle, S.M. & Wickner, S. Trends Biochem. Sci. 34, 40–48 (2009).

    Article  CAS  Google Scholar 

  5. Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F. & Kuriyan, J. Science 276, 431–435 (1997).

    Article  CAS  Google Scholar 

  6. Zhu, X. et al. Science 272, 1606–1614 (1996).

    Article  CAS  Google Scholar 

  7. Lee, S. et al. Cell 115, 229–240 (2003).

    Article  CAS  Google Scholar 

  8. Rosenzweig, R., Moradi, S., Zarrine-Afsar, A., Glover, J.R. & Kay, L.E. Science 339, 1080–1083 (2013).

    Article  CAS  Google Scholar 

  9. Sprangers, R. & Kay, L.E. Nature 445, 618–622 (2007).

    Article  CAS  Google Scholar 

  10. Ruschak, A.M. & Kay, L.E. Proc. Natl. Acad. Sci. USA 109, E3454–E3462 (2012).

    Article  CAS  Google Scholar 

  11. Religa, T.L., Sprangers, R. & Kay, L.E. Science 328, 98–102 (2010).

    Article  CAS  Google Scholar 

  12. Gelis, I. et al. Cell 131, 756–769 (2007).

    Article  CAS  Google Scholar 

  13. Zhuravleva, A., Clérico, E.M. & Gierasch, L.M. Cell 151, 1296–1307 (2012).

    Article  CAS  Google Scholar 

  14. Hamel, D.J. & Dahlquist, F. J. Am. Chem. Soc. 127, 9676–9677 (2005).

    Article  CAS  Google Scholar 

  15. Takahashi, H. et al. J. Biomol. NMR 34, 167–177 (2006).

    Article  CAS  Google Scholar 

  16. Chen, L. et al. Cell Rep. doi:10.1016/j.celrep.2013.02.025 (in the press).

  17. Battiste, J.L. & Wagner, G. Biochemistry 39, 5355–5365 (2000).

    Article  CAS  Google Scholar 

  18. Clore, G.M., Tang, C. & Iwahara, J. Curr. Opin. Struct. Biol. 17, 603–616 (2007).

    Article  CAS  Google Scholar 

  19. Wendler, P. et al. Cell 131, 1366–1377 (2007).

    Article  CAS  Google Scholar 

  20. Saibil, H.R. Science 339, 1040–1041 (2013).

    Article  CAS  Google Scholar 

Download references

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Authors and Affiliations

  1. Tomohide Saio and Charalampos G. Kalodimos are at the Center for Integrative Proteomics Research and Department of Chemistry & Chemical Biology, Rutgers University, Piscataway, New Jersey, USA.,

    Tomohide Saio & Charalampos G Kalodimos

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  1. Tomohide Saio
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  2. Charalampos G Kalodimos
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Correspondence to Charalampos G Kalodimos.

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The authors declare no competing financial interests.

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Saio, T., Kalodimos, C. NMR disentangles a dynamic disaggregase machinery. Nat Struct Mol Biol 20, 409–410 (2013). https://doi.org/10.1038/nsmb.2551

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