Newly Folded Substrates Inside the Molecular Cage of the HtrA Chaperone DegQ

Overview

Journal Nat Struct Mol Biol

Specialties Cell Biology
Molecular Biology

Date 2012 Jan 17

PMID 22245966

Citations 31

Authors

Helene Malet

Flavia Canellas

Justyna Sawa

Jun Yan

Konstantinos Thalassinos

Michael Ehrmann

Tim Clausen

Helen R Saibil

Affiliations

Soon will be listed here.

Abstract

The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function.

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