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Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

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Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

Auteurs : Hélène Malet [Royaume-Uni] ; Flavia Canellas [Autriche] ; Justyna Sawa [Autriche] ; Jun Yan [Royaume-Uni] ; Konstantinos Thalassinos [Royaume-Uni] ; Michael Ehrmann [Allemagne] ; Tim Clausen [Autriche] ; Helen R. Saibil [Royaume-Uni]

Source :

Nature Structural & Molecular Biology [ 1545-9993 ] ; 2012-02.

RBID : ISTEX:12F9CDCE4E1ADA8B1A83DFDB5E323D1567B5621C

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.

HtrA proteins have chaperone and protease activities, but how they bind and fold their substrates is poorly understood. New cryo-EM analyses of a protease-defective bacterial DegQ mutant in complex with several different substrates provide a structural model of HtrA proteins in their chaperone mode.

Url:

https://api.istex.fr/ark:/67375/GT4-MVLZ73Z6-4/fulltext.pdf

DOI: 10.1038/nsmb.2210

Affiliations:

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Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

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Abstract

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