Key Information

Date & Time: October 10th, 2022 – kl 14.15
Registration deadline: October 9th
Location: Seminar Berzelius, Department of Chemistry, UiO
Zoom Registration: Available at bottom of page
Contact: Ute Krengel

Speaker: Wayne Hendrickson

Wayne Hendrickson of Columbia University in New York City is coming to UiO! You can read more about Wayne and his research here and here. The title and abstract for his presentation can be found below. Participants are encouraged to come to join the event in person, but there will also be a Zoom Link for those who are unable to attend. You must register in advance for the Zoom Link, which can be done at the bottom of this page.

Title: Allosteric control of Hsp70 protein folding activity

Heat-shock proteins of 70 kDa (Hsp70s) are vital for all of life and notably important for protein folding.  Hsp70s use iterations of ATP binding and hydrolysis in one domain to control the binding and release of client polypeptides in a second domain.  ATP-fueled cycles of Hsp70 activity promote proper protein folding by blocking or reversing the aggregation of misfolded intermediates, often stress induced.  To explain functional characteristics of Hsp70 DnaK and structure-inspired mutants, we developed a theoretical model of allosteric equilibria among

Hsp70 conformational states: when in ATP, a restraining state (R) restricts ATP hydrolysis and does not bind client peptides, whereas a stimulating state (S) hydrolyzes ATP rapidly and binds substrates well but with rapid binding kinetics.  ATP hydrolysis uncouples the allosteric interactions, and clients are then caught in tight complexes until ejected by ATP rebinding.  This model for allosteric regulation is supported by structures in the postulated S state, by biochemical tests and additional mutations, and by in cristallo hydrolysis reactions in the ATP-binding domain.

Zoom Registration