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Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi‐domain proteins in Escherichia coli
Author(s) -
Gupta Rashmi,
Lakshmipathy Sathish Kumar,
Chang Hung-Chun,
Etchells Stephanie A.,
Hartl F. Ulrich
Publication year - 2010
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.2010.07.036
Subject(s) - protein folding , chaperone (clinical) , mutant , microbiology and biotechnology , folding (dsp implementation) , chemistry , escherichia coli , luciferase , biochemistry , biology , medicine , transfection , pathology , electrical engineering , gene , engineering
Recombinant expression of eukaryotic proteins in bacteria often results in misfolding and aggregation. The ribosome‐binding Trigger factor (TF) is the first molecular chaperone that interacts with nascent polypeptide chains in bacteria. Here we show that mutant TF lacking the PPIase domain (TFNC) is more efficient than wild‐type TF in enhancing the folding yield of multi‐domain proteins such as firefly luciferase. We find that TFNC has a shorter residence time on nascent chains, thus facilitating co‐translational folding. By delaying folding relative to translation, the PPIase domain may increase the propensity of misfolding for certain eukaryotic proteins that rely on a mechanism of co‐translational, domain‐wise folding.