Related Experiment Video
Updated: Nov 20, 2025

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug
Vladimir Baytshtok1, Xue Fei1, Tsai-Ting Shih1
1Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Abstract:
At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU6 unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV12 peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis.
Related Concept Videos
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Single-Strand DNA Binding Proteins

