Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins

• DOI: 10.1073/pnas.0805464105
• Publication Date: 2008-08-13T03:29:08Z
• Authors: Jiansen Jiang; Xuefeng Zhang; Yong Chen; Yi Wu; Z. Hong Zhou; Zengyi Chang; Sen-Fang Sui
• Keywords: Chaperone (clinical)

Cells use molecular chaperones and proteases to implement the essential quality control mechanism of proteins. The DegP (HtrA) protein, for survival Escherichia coli cells at elevated temperatures with homologues found in almost all organisms uniquely has both functions. Here we report a activate functions via formation large cage-like 12- 24-mers after binding substrate Cryo-electron microscopic biochemical studies revealed that oligomers are consistently assembled by blocks trimers, pairwise PDZ1-PDZ2 interactions between neighboring trimers. Such simultaneously eliminate inhibitory effects PDZ2 domain. Additionally, were also observed extracts E. cells, strongly implicating their physiological importance.