Ontology highlight
ABSTRACT:
SUBMITTER: Rehn A
PROVIDER: S-EPMC7057950 | biostudies-literature | 2020 Mar
REPOSITORIES: biostudies-literature
Rehn Alexandra A Lawatscheck Jannis J Jokisch Marie-Lena ML Mader Sophie L SL Luo Qi Q Tippel Franziska F Blank Birgit B Richter Klaus K Lang Kathrin K Kaila Ville R I VRI Buchner Johannes J
Nature communications 20200305 1
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 ...[more]