Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis
Huston, Willa, Tyndall, Joel, Lott, William, Stansfield, Scott, & Timms, Peter (2011) Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis. PLoS ONE, 6(9), pp. 1-10.
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.
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|Item Type:||Journal Article|
|Subjects:||Australian and New Zealand Standard Research Classification > AGRICULTURAL AND VETERINARY SCIENCES (070000)|
Australian and New Zealand Standard Research Classification > MEDICAL AND HEALTH SCIENCES (110000)
|Divisions:||Current > QUT Faculties and Divisions > Faculty of Health|
Current > Institutes > Institute of Health and Biomedical Innovation
|Copyright Owner:||Copyright 2011 the authors|
|Copyright Statement:||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.|
|Deposited On:||19 Jul 2012 16:32|
|Last Modified:||09 Apr 2014 22:21|
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