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

Huston, Wilhelmina M., Swedberg, Joakim, Harris, Jonathan M., Walsh, Terence P., Mathews, Sarah A. and Timms, Peter (2007) The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 degrees C. FEBS Letters, 581 18: 3382-3386. doi:10.1016/j.febslet.2007.06.039


Author Huston, Wilhelmina M.
Swedberg, Joakim
Harris, Jonathan M.
Walsh, Terence P.
Mathews, Sarah A.
Timms, Peter
Title The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 degrees C
Formatted title
The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C
Journal name FEBS Letters   Check publisher's open access policy
ISSN 0014-5793
1873-3468
Publication date 2007-07-24
Year available 2007
Sub-type Article (original research)
DOI 10.1016/j.febslet.2007.06.039
Open Access Status Not yet assessed
Volume 581
Issue 18
Start page 3382
End page 3386
Total pages 5
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Subject 1304 Biophysics
1315 Structural Biology
1303 Biochemistry
1312 Molecular Biology
1311 Genetics
1307 Cell Biology
Abstract 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 α-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.
Formatted abstract
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 α-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.
Keyword HtrA
Serine protease
Chaperone
Chlamydia
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 29 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 30 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 06 Sep 2011, 01:07:45 EST by Susan Allen on behalf of Institute for Molecular Bioscience