FEBS Letters
Volume 584, Issue 16 , Pages 3620-3624, 20 August 2010

Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli

Edited by Aleksander Benjak

  • Rashmi Gupta
    • ,
  • Sathish Kumar Lakshmipathy

      Affiliations

    • Present address: Department of Intracellular Proteolysis, Max-Delbrück-Centrum für Molekulare Medizin (MDC), Robert-Rössle-Str. 10, 13092 Berlin, Germany.
    • ,
  • Hung-Chun Chang

      Affiliations

    • Present address: Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
    • ,
  • Stephanie A. Etchells

      Affiliations

    • Present address: Canadian Intellectual Property Office, Industry Canada, 50 Victoria Street, Gatineau, Canada QC K1A OC9.
    • ,
  • F. Ulrich Hartl

      Affiliations

    • Corresponding Author InformationCorresponding author. Fax: +49 89 8578 2211.

Department of Cellular Biochemistry, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany

Received 8 July 2010; received in revised form 20 July 2010; accepted 20 July 2010. published online 26 July 2010.

Abstract 

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.

Keywords: Trigger factor, Ribosome, Chaperone, Luciferase, Multi-domain

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PII: S0014-5793(10)00594-6

doi:10.1016/j.febslet.2010.07.036

FEBS Letters
Volume 584, Issue 16 , Pages 3620-3624, 20 August 2010

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