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The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37 °C
Author(s) -
Huston Wilhelmina M.,
Swedberg Joaquim E.,
Harris Jonathan M.,
Walsh Terence P.,
Mathews Sarah A.,
Timms Peter
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.039
Subject(s) - chaperone (clinical) , protease , chlamydia trachomatis , serine protease , biology , microbiology and biotechnology , biochemistry , enzyme , chemistry , virology , medicine , pathology
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.