24-26 September 2020
Lima, Perú
America/Lima timezone
Share our event through the following link: https://indico.uni.edu.pe/e/Meeting-of-Physics-2020

A finely tuned molecular motor: power generation and mechanical efficiency of a protein degradation machine

24 Sep 2020, 13:40
20m
Lima, Perú

Lima, Perú

Centro de Investigación de la Facultad de Ciencias Universidad Nacional de Ingeniería
video conference Materials Science and Nanotechnology Applied Physics

Speaker

Dr Piere Rodriguez Aliaga (Stanford University)

Description

Molecular motors transduce chemical energy –usually from ATP hydrolysis– into directed motion and mechanical work, which is used to perform key functions in almost every cellular process. Molecular motors are particularly important in the maintenance of cellular proteostasis, i.e. the equilibrium between protein synthesis and degradation. ATP-dependent proteases of the AAA+ family, such as ClpXP from Escherichia coli and the eukaryotic 26S proteasome, play a central role in protein degradation. Given its extensive biochemical and structural characterization, ClpXP is a paradigm for the study of the operating principles of eukaryotic and prokaryotic protease machines of the AAA+ family. However, the molecular mechanism by which ClpXP couples the energy from ATP hydrolysis into mechanical work is still poorly understood. Here we used biochemical and single-molecule assays with optical tweezers to directly probe the operation of ClpXP as it unfolds and translocates its protein substrate. We observe that ClpXP operates with constant “rpm” but uses different “gears”, and provide insights about how evolution has tuned the structure and sequence of this motor to maximize its power production and mechanical efficiency.

Primary authors

Dr Piere Rodriguez Aliaga (Stanford University) Dr Carlos Bustamante (University of California at Berkeley) Dr Andreas Martin (University of California at Berkeley)

Presentation Materials

There are no materials yet.
Your browser is out of date!

Update your browser to view this website correctly. Update my browser now

×