Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis

W M Huston; J D A Tyndall; W B Lott; S H Stansfield; Peter Timms

doi:10.1371/journal.pone.0024547

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Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis

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Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis

W M Huston, J D A Tyndall, W B Lott, S H Stansfield and Peter Timms

PLoS One, Vol.6(9), e24547

2011

DOI: https://doi.org/10.1371/journal.pone.0024547

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Abstract

Chlamydia trachomatis

DegP, a member of the HtrA family of proteins, conducts critical bacterial protein quality control by both chaperone and proteolysis activities. The regulatory mechanisms controlling these two distinct activities, however, are unknown. DegP activation is known to involve a unique mechanism of allosteric binding, conformational changes and oligomer formation. We have uncovered a novel role for the residues at the PDZ1:protease interface in oligomer formation specifically for chaperone substrates of Chlamydia trachomatis HtrA (DegP homolog). We have demonstrated that CtHtrA proteolysis could be activated by allosteric binding and oligomer formation. The PDZ1 activator cleft was required for the activation and oligomer formation. However, unique to CtHtrA was the critical role for residues at the PDZ1:protease interface in oligomer formation when the activator was an in vitro chaperone substrate. Furthermore, a potential in vivo chaperone substrate, the major outer membrane protein (MOMP) from Chlamydia, was able to activate CtHtrA and induce oligomer formation. Therefore, we have revealed novel residues involved in the activation of CtHtrA which are likely to have important in vivo implications for outer membrane protein assembly. © 2011 Huston et al.

Details

Title: Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis
Authors: W M Huston (Author) - Queensland University of Technology
J D A Tyndall (Author) - University of Otago, New Zealand
W B Lott (Author) - Queensland University of Technology
S H Stansfield (Author) - Queensland University of Technology
Peter Timms (Author) - Queensland University of Technology
Publication details: PLoS One, Vol.6(9), e24547; 10
Publisher: Public Library of Science
Date published: 2011
DOI: 10.1371/journal.pone.0024547
ISSN: 1932-6203
Copyright note: Copyright © 2011 Huston et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Organisation Unit: University of the Sunshine Coast, Queensland; Centre for Bioinnovation
Language: English
Record Identifier: 99448860102621
Output Type: Journal article

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Web Of Science research areas: Biochemistry & Molecular Biology

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