Dynamics of ribosomes and release factors during translation termination in 
E-coli.

Adio, S.; Sharma, H.; Senyushkina, T.; Karki, P.; Maracci, C.; Wohlgemuth, I.; Holtkamp, W.; Peske, F.; Rodnina, M. V.

doi:10.7554/eLife.34252

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Dynamics of ribosomes and release factors during translation termination in E-coli.

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Adio, S.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons194933

Sharma, H.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons31223

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

/persons/resource/persons206931

Karki, P.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons135076

Maracci, C.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16047

Wohlgemuth, I.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons32550

Holtkamp, W.
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/persons15723

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

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Citation

Adio, S., Sharma, H., Senyushkina, T., Karki, P., Maracci, C., Wohlgemuth, I., et al. (2018). Dynamics of ribosomes and release factors during translation termination in E-coli. eLife, 7: e34252. doi:10.7554/eLife.34252.

Cite as: https://hdl.handle.net/21.11116/0000-0001-9266-7

Abstract

Release factors RF1 and RF2 promote hydrolysis of peptidyl-tRNA during translation termination. The GTPase RF3 promotes recycling of RF1 and RF2. Using single molecule FRET and biochemical assays, we show that ribosome termination complexes that carry two factors, RF1 RF3 or RF2 RF3, are dynamic and fluctuate between non-rotated and rotated states, whereas each factor alone has its distinct signature on ribosome dynamics and conformation. Dissociation of RF1 depends on peptide release and the presence of RF3, whereas RF2 can dissociate spontaneously. RF3 binds in the GTP-bound state and can rapidly dissociate without GTP hydrolysis from termination complex carrying RF1. In the absence of RF1, RF3 is stalled on ribosomes if GTP hydrolysis is blocked. Our data suggest how the assembly of the ribosome RF1 RF3 GTP complex, peptide release, and ribosome fluctuations promote termination of protein synthesis and recycling of the release factors.