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  • Rehn, Alexandra (author)

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020-03-05
  • Springer Science and Business Media LLC,2020
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:su-183598
  • https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-183598URI
  • https://doi.org/10.1038/s41467-020-15048-8DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Methylation of a conserved lysine in C-terminal domain of the molecular chaperone Hsp90 was shown previously to affect its in vivo function. However, the underlying mechanism remained elusive. Through a combined experimental and computational approach, this study shows that this site is very sensitive to sidechain modifications and crucial for Hsp90 activity in vitro and in vivo. Our results demonstrate that this particular lysine serves as a switch point for the regulation of Hsp90 functions by influencing its conformational cycle, ATPase activity, co-chaperone regulation, and client activation of yeast and human Hsp90. Incorporation of the methylated lysine via genetic code expansion specifically shows that upon modification, the conformational cycle of Hsp90 is altered. Molecular dynamics simulations including the methylated lysine suggest specific conformational changes that are propagated through Hsp90. Thus, methylation of the C-terminal lysine allows a precise allosteric tuning of Hsp90 activity via long distances. Methylation of a lysine residue in Hsp90 is a recently discovered post-translational modification but the mechanistic effects of this modification have remained unknown so far. Here the authors combine biochemical and biophysical approaches, molecular dynamics (MD) simulations and functional experiments with yeast and show that this lysine is a switch point, which specifically modulates conserved Hsp90 functions including co-chaperone regulation and client activation.

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Added entries (persons, corporate bodies, meetings, titles ...)

  • Lawatscheck, Jannis (author)
  • Jokisch, Marie-Lena (author)
  • Mader, Sophie L. (author)
  • Luo, Qi (author)
  • Tippel, Franziska (author)
  • Blank, Birgit (author)
  • Richter, Klaus (author)
  • Lang, Kathrin (author)
  • Kaila, Ville R. I.Stockholms universitet,Institutionen för biokemi och biofysik,Technische Universität München, Germany(Swepub:su)vika1812 (author)
  • Buchner, Johannes (author)
  • Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

Related titles

  • In:Nature Communications: Springer Science and Business Media LLC11:12041-1723

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