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Article

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

Nature communications - 5 Mar 2020

Rehn Alexandra, Lawatscheck Jannis, Jokisch Marie-Lena, Mader Sophie L, Luo Qi, Tippel Franziska, Blank Birgit, Richter Klaus, Lang Kathrin, Kaila Ville R I, Buchner Johannes

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32139682
DOI: 10.1038/s41467-020-15048-8
PMCID: PMC7057950

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