Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.

ABSTRACT: DegP is an oligomeric protein with dual protease and chaperone activity that regulates protein homeostasis and virulence factor trafficking in the periplasm of gram-negative bacteria. A number of oligomeric architectures adopted by DegP are thought to facilitate its function. For example, DegP can form a "resting" hexamer when not engaged to substrates, mitigating undesired proteolysis of cellular proteins. When bound to substrate proteins or lipid membranes, DegP has been shown to populate a variety of cage- or bowl-like oligomeric states that have increased proteolytic activity. Though a number of DegP's substrate-engaged structures have been robustly characterized, detailed mechanistic information underpinning its remarkable oligomeric plasticity and the corresponding interplay between

SUBMITTER: Harkness RW 

PROVIDER: S-EPMC8364167 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature