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Journal Article

Ribosome rearrangements at the onset of translational bypassing.

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Samatova,  E. N.
Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Klimova,  M.
Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Agirrezabala, X., Samatova, E. N., Klimova, M., Zamora, M., Gil-Carton, D., Rodnina, M. V., et al. (2017). Ribosome rearrangements at the onset of translational bypassing. Science Advances, 3(6): e1700147. doi:10.1126/sciadv.1700147.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-7F87-F
Abstract
Bypassing is a recoding event that leads to the translation of two distal open reading frames into a single polypeptide chain. We present the structure of a translating ribosome stalled at the bypassing take-off site of gene 60 of bacteriophage T4. The nascent peptide in the exit tunnel anchors the P-site peptidyl-tRNAGly to the ribosome and locks an inactive conformation of the peptidyl transferase center (PTC). The mRNA forms a short dynamic hairpin in the decoding site. The ribosomal subunits adopt a rolling conformation in which the rotation of the small subunit around its long axis causes the opening of the A-site region. Together, PTC conformation and mRNA structure safeguard against premature termination and read-through of the stop codon and reconfigure the ribosome to a state poised for take-off and sliding along the noncoding mRNA gap.