Vie de l'IBPC

The bacterial Hsp90 chaperone: mechanism, partners, and function

 Olivier Genest

Laboratoire de Bioénergétique et Ingénierie des Protéines (BIP)
UMR 7281, CNRS Aix Marseille Université


invité  par Philippe Meyer



le lundi 23  janvier 2017 à 11h - Salle de conférence de l'IBPC - 3^e étage

Molecular chaperones are proteins that assist the folding of other proteins. In stress conditions, they are crucial as proteins become misfolded. The Hsp90 chaperone is present in almost all living organisms and is essential in eukaryotes. In contrast, Hsp90 is dispensable in E. coli and few client proteins have been identified for bacterial Hsp90. The goal of my work is to better understand the role and mechanism of action of bacterial Hsp90. Using Hsp90 from E. coli, we found that Hsp90 collaborates with the DnaK chaperone system to remodel proteins. This collaboration involves a direct interaction between the two chaperones. We also identified functional regions of Hsp90 that are important for client protein binding and for DnaK binding. Finally, we found that bacterial Hsp90 is essential in stress conditions in vivo using another model bacteria, Shewanella oneidensis. This phenotype allowed us to get insights into the functions and client proteins of bacterial Hsp90.