Prokaryotic DegP functions as an ATPase-independent protease chaperone complex that is activated by oligomerization. Site-directed mutagenesis, combined with refolding and oligomerization studies of chemically denatured DegP, shows how substrates trigger the conversion of the resting conformation into the active conformation.
- Melisa Merdanovic
- Nicolette Mamant
- Michael Ehrmann
