Folding Optimization in Vivo Uncovers New Chaperones

Christopher W. Lennon*, Maike Thamsen, Elias T. Friman, Austin Cacciaglia, Veronika Sachsenhauser, Frieda A. Sorgenfrei, Milena A. Wasik, James C.A. Bardwell

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

By employing a genetic selection that forces the cell to fold an unstable, aggregation-prone test protein in order to survive, we have generated bacterial strains with enhanced periplasmic folding capacity. These strains enhance the soluble steady-state level of the test protein. Most of the bacterial variants we isolated were found to overexpress one or more periplasmic proteins including OsmY, Ivy, DppA, OppA, and HdeB. Of these proteins, only HdeB has convincingly been previously shown to function as chaperone in vivo. By giving bacteria the stark choice between death and stabilizing a poorly folded protein, we have now generated designer bacteria selected for their ability to stabilize specific proteins.

Original languageEnglish
Pages (from-to)2983-2994
Number of pages12
JournalJournal of Molecular Biology
Issue number18
Early online date21 May 2015
Publication statusPublished - 11 Sept 2015

Keywords / Materials (for Non-textual outputs)

  • chaperone discovery
  • folding sensor
  • periplasm
  • protein folding
  • proteostasis


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