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Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
Author(s) -
Houry Walid A.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.00499
Subject(s) - chaperone (clinical) , biology , microbiology and biotechnology , protein degradation , proteolysis , signal transducing adaptor protein , gene , biochemistry , enzyme , medicine , pathology
A functional association was uncovered between the ribosome‐associated trigger factor (TF) chaperone and the ClpXP degradation complex in bacteria. Bioinformatic analyses demonstrated conservation of the close proximity of tig , gene coding for TF, and genes coding for ClpXP suggesting a functional association. Effect of TF on ClpXP‐dependent degradation varied based on the nature of substrate. While degradation of some substrates was slowed down or unaffected by TF, surprisingly, TF increased the degradation rate for a third class of substrates. These include λ phage replication protein λO, master regulator of stationary phase RpoS, and SsrA‐tagged proteins. Globally, TF enhances the degradation of about 2% of newly synthesized proteins. TF was found to interact through multiple sites with ClpX in a highly dynamic fashion to promote protein degradation. This chaperone‐protease cooperation constitutes a unique and likely ancestral aspect of cellular protein homeostasis in which TF acts as an adaptor for ClpXP. Support or Funding Information Canadian Institutes of Health Research