Article
Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.
FEBS letters - 20 Aug 2010
Gupta Rashmi, Lakshmipathy Sathish Kumar, Chang Hung-Chun, Etchells Stephanie A, Hartl F Ulrich
Abstract excerpt
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...
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