The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C

W M Huston; J E Swedberg; J M Harris; T P Walsh; S A Mathews; Peter Timms

doi:10.1016/j.febslet.2007.06.039

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The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C

Journal article

Peer reviewed

The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C

W M Huston, J E Swedberg, J M Harris, T P Walsh, S A Mathews and Peter Timms

FEBS Letters, Vol.581(18), pp.3382-3386

2007

DOI: https://doi.org/10.1016/j.febslet.2007.06.039

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Abstract

HtrA

serine protease

chaperone

chlamydia

Characterization of the protease, HtrA, from pathogen Chlamydia trachomatis is presented. The purified recombinant protein was a serine endoprotease, specific for unfolded proteins, and temperature activated above 34 °C. Chaperone activity was observed, although this appeared target-dependent. Inactive protease (S247A) was able to chaperone insulin B-chain, irrespective of temperature, but at 30 °C only HtrA and not S247A displayed significant chaperone activity for ?-lactalbumin. These data demonstrate that chaperone activity may involve functional protease domain and that C. trachomatis HtrA functions as both a chaperone and protease at 37 °C. These properties are consistent with the developmental cycle of this obligate intracellular bacterium. © 2007 Federation of European Biochemical Societies.

Details

Title: The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C
Authors: W M Huston (Author) - Queensland University of Technology
J E Swedberg (Author) - Queensland University of Technology
J M Harris (Author) - Queensland University of Technology
T P Walsh (Author) - Queensland University of Technology
S A Mathews (Author) - Queensland University of Technology
Peter Timms (Author) - Queensland University of Technology
Publication details: FEBS Letters, Vol.581(18), pp.3382-3386
Publisher: John Wiley & Sons Ltd.
DOI: 10.1016/j.febslet.2007.06.039
ISSN: 0014-5793
Organisation Unit: Centre for Bioinnovation; University of the Sunshine Coast, Queensland
Language: English
Record Identifier: 99449977102621
Output Type: Journal article

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