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Molecular biology

Mature proteins braced by a chaperone

Nature volume 539, pages 361–362 (2016)Cite this article

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Hsp70 chaperone molecules help other proteins to fold, and were thought to bind mainly to unfolded proteins. Single-molecule experiments now suggest that Hsp70s can also stabilize almost fully folded proteins. See Letter p.448

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Figure 1: Different roles of Hsp70s in protein folding.

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References

  1. Balchin, D., Hayer-Hartl, M. & Hartl, F. U. Science 353, aac4354 (2016).

    Article  PubMed  Google Scholar 

  2. Mayer, M. P. & Bukau, B. Cell. Mol. Life Sci. 62, 670–684 (2005).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Boorstein, W. R., Ziegelhoffer, T. & Craig, E. A. J. Mol. Evol. 38, 1–17 (1994).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Clerico, E. M., Tilitsky, J. M., Meng, W. & Gierasch, L. M. J. Mol. Biol. 427, 1575–1588 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Mashaghi, A. et al. Nature 539, 448–451 (2016).

    Article  ADS  CAS  PubMed  Google Scholar 

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

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  7. Flynn, G. C., Chappell, T. G. & Rothman, J. E. Science 245, 385–390 (1989).

    Article  ADS  CAS  PubMed  Google Scholar 

  8. Schmid, D., Baici, A., Gehring, H. & Christen, P. Science 263, 971–973 (1994).

    Article  ADS  CAS  PubMed  Google Scholar 

  9. Qi, R. et al. Nature Struct. Mol. Biol. 20, 900–907 (2013).

    Article  CAS  Google Scholar 

  10. Kityk, R., Kopp, J., Sinning, I. & Mayer, M. P. Mol. Cell 48, 863–874 (2012).

    Article  CAS  PubMed  Google Scholar 

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

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Kampinga, H. H. & Craig, E. A. Nature Rev. Mol. Cell Biol. 11, 579–592 (2010).

    Article  CAS  Google Scholar 

  13. Bracher, A. & Verghese, J. Front. Mol. Biosci. 2, 10 (2015).

    Article  PubMed  PubMed Central  Google Scholar 

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Author notes

  1. Elizabeth A. Craig is in the Department of Biochemistry, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA.

Authors and Affiliations

  1. Qinglian Liu is in the Department of Physiology and Biophysics, Virginia Commonwealth University, Richmond, Virginia 23298-0551, USA.,

    Qinglian Liu & Elizabeth A. Craig

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  1. Qinglian Liu
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  2. Elizabeth A. Craig
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Correspondence to Qinglian Liu or Elizabeth A. Craig.

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Liu, Q., Craig, E. Mature proteins braced by a chaperone. Nature 539, 361–362 (2016). https://doi.org/10.1038/nature20470

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