Principal Investigator Tania Baker
Timely disassembly of higher order protein-DNA complexes is essential for the proper control of biological processes. We became interested in protein disassembly when we found that the ClpX protein, a member of the Clp/Hsp100 family, promotes a protein-remodeling reaction that helps release the transposase from the DNA following recombination. This work contributed to the conclusion that Clp/Hsp100 proteins are chaperones specifically suited for disassembling or disaggregating other proteins. ClpX also functions as an essential component of the ClpXP protease. The ClpP component is a cylindrical protein chamber that provides the peptidase-active sites to degrade proteins that are chosen and delivered by ClpX. To increase our understanding of Clp/Hsp100 protein function, we are focusing on four research areas.