Dynamic Behavior of Trigger Factor on the Ribosome

J. Deeng, K. Y. Chan, E. O. van der Sluis, O. Berninghausen, W. Han, J. Gumbart, K. Schulten, B. Beatrix, R. Beckmann

Research output: Contribution to journalArticlepeer-review


Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ribosome-binding domain (RBD) mainly to ribosomal protein uL23 at the tunnel exit on the large ribosomal subunit. Whereas earlier structural data suggested that TF binds as a rigid molecule to the ribosome, recent comparisons of structural data on substrate-bound, ribosome-bound, and TF in solution from different species suggest that this chaperone is a rather flexible molecule. Here, we present two cryo-electron microscopy structures of TF bound to ribosomes translating an mRNA coding for a known TF substrate from Escherichia coli of a different length. The structures reveal distinct degrees of flexibility for the different TF domains, a conformational rearrangement of the RBD upon ribosome binding, and an increase in rigidity within TF when the NC is extended. Molecular dynamics simulations agree with these data and offer a molecular basis for these observations.

Original languageEnglish (US)
Pages (from-to)3588-3602
Number of pages15
JournalJournal of Molecular Biology
Issue number18
StatePublished - Sep 11 2016


  • chaperones
  • cryo-electron microscopy
  • molecular dynamics simulation
  • protein folding
  • ribosome-binding domain

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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