TCB Publications - Abstract

Julian Deeng, Kwok-Yan Chan, Eli O. van der Sluis, Lukas Bischoff, Otto Berninghausen, Wei Han, James Gumbart, Klaus Schulten, Birgitta Beatrix, and Roland Beckmann. Dynamic behavior of trigger factor on the ribosome. Journal of Molecular Biology, 428:3588-3602, 2016.

DEEN2016 Trigger factor is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chains 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-EM structures of TF bound to ribosomes translating an mRNA coding for a known TF substrate from E. coli of 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 nascent chain is extended. Molecular dynamics simulations agree with these data and offer a molecular basis for these observations.

Download Full Text

The manuscripts available on our site are provided for your personal use only and may not be retransmitted or redistributed without written permissions from the paper's publisher and author. You may not upload any of this site's material to any public server, on-line service, network, or bulletin board without prior written permission from the publisher and author. You may not make copies for any commercial purpose. Reproduction or storage of materials retrieved from this web site is subject to the U.S. Copyright Act of 1976, Title 17 U.S.C.

Download full text: Request a Copy, Journal