A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
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 experim...
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Nature Portfolio
2020
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oai:doaj.org-article:e58f3663006545cf9df6166e474e1b1b2021-12-02T17:31:10ZA methylated lysine is a switch point for conformational communication in the chaperone Hsp9010.1038/s41467-020-15048-82041-1723https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15048-8https://doaj.org/toc/2041-1723Methylation 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.Alexandra RehnJannis LawatscheckMarie-Lena JokischSophie L. MaderQi LuoFranziska TippelBirgit BlankKlaus RichterKathrin LangVille R. I. KailaJohannes BuchnerNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020) |
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Science Q Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
description |
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. |
format |
article |
author |
Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner |
author_facet |
Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner |
author_sort |
Alexandra Rehn |
title |
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
title_short |
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
title_full |
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
title_fullStr |
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
title_full_unstemmed |
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
title_sort |
methylated lysine is a switch point for conformational communication in the chaperone hsp90 |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b |
work_keys_str_mv |
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