Send to

Choose Destination
FEBS Lett. 2007 Jul 24;581(18):3382-6. Epub 2007 Jun 26.

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

Author information

Institute of Health and Biomedical Innovation and School of Life Sciences, Faculty of Science, Queensland University of Technology, Brisbane, Australia.


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 degrees 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 degrees C only HtrA and not S247A displayed significant chaperone activity for alpha-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 degrees C. These properties are consistent with the developmental cycle of this obligate intracellular bacterium.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center