English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome.

MPS-Authors
/persons/resource/persons31223

Senyushkina,  T.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons40304

Peske,  F.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16038

Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15723

Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

2156321.pdf
(Publisher version), 2MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Adio, S., Senyushkina, T., Peske, F., Fischer, N., Wintermeyer, W., & Rodnina, M. V. (2015). Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome. Nature Communications, 6: 7442. doi:10.1038/ncomms8442.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0026-DBB8-2
Abstract
The coupled translocation of transfer RNA and messenger RNA through the ribosome entails large-scale structural rearrangements, including step-wise movements of the tRNAs. Recent structural work has visualized intermediates of translocation induced by elongation factor G (EF-G) with tRNAs trapped in chimeric states with respect to 30S and 50S ribosomal subunits. The functional role of the chimeric states is not known. Here we follow the formation of translocation intermediates by single-molecule fluorescence resonance energy transfer. Using EF-G mutants, a non-hydrolysable GTP analogue, and fusidic acid, we interfere with either translocation or EF-G release from the ribosome and identify several rapidly interconverting chimeric tRNA states on the reaction pathway. EF-G engagement prevents backward transitions early in translocation and increases the fraction of ribosomes that rapidly fluctuate between hybrid, chimeric and posttranslocation states. Thus, the engagement of EF-G alters the energetics of translocation towards a flat energy landscape, thereby promoting forward tRNA movement.