Translation dynamics in human cells visualized at high resolution reveal cancer drug action

Author:

Xing Huaipeng12ORCID,Taniguchi Reiya1ORCID,Khusainov Iskander1ORCID,Kreysing Jan Philipp13ORCID,Welsch Sonja4ORCID,Turoňová Beata1ORCID,Beck Martin15ORCID

Affiliation:

1. Department of Molecular Sociology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.

2. Faculty of Biochemistry, Chemistry and Pharmacy, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.

3. IMPRS on Cellular Biophysics, 60438 Frankfurt am Main, Germany.

4. Central Electron Microscopy Facility, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.

5. Institute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.

Abstract

Ribosomes catalyze protein synthesis by cycling through various functional states. These states have been extensively characterized in vitro, but their distribution in actively translating human cells remains elusive. We used a cryo–electron tomography-based approach and resolved ribosome structures inside human cells with high resolution. These structures revealed the distribution of functional states of the elongation cycle, a Z transfer RNA binding site, and the dynamics of ribosome expansion segments. Ribosome structures from cells treated with Homoharringtonine, a drug used against chronic myeloid leukemia, revealed how translation dynamics were altered in situ and resolve the small molecules within the active site of the ribosome. Thus, structural dynamics and drug effects can be assessed at high resolution within human cells.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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