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Journal Article

Active role of elongation factor G in maintaining the mRNA reading frame during translation.

MPS-Authors
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Peng,  B. Z.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Bock,  L. V.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Belardinelli,  R.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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

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Grubmüller,  H.
Department of Theoretical and Computational Biophysics, 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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Fulltext (public)

3186671.pdf
(Publisher version), 2MB

Supplementary Material (public)

3186671_Suppl.DC1
(Supplementary material), 57KB

Citation

Peng, B. Z., Bock, L. V., Belardinelli, R., Peske, F., Grubmüller, H., & Rodnina, M. V. (2019). Active role of elongation factor G in maintaining the mRNA reading frame during translation. Science Advances, 5(12): eaax8030. doi:10.1126/sciadv.aax8030.


Cite as: http://hdl.handle.net/21.11116/0000-0005-7983-F
Abstract
During translation, the ribosome moves along the mRNA one codon at a time with the help of elongation factor G (EF-G). Spontaneous changes in the translational reading frame are extremely rare, yet how the precise triplet-wise step is maintained is not clear. Here, we show that the ribosome is prone to spontaneous frameshifting on mRNA slippery sequences, whereas EF-G restricts frameshifting. EF-G helps to maintain the mRNA reading frame by guiding the A-site transfer RNA during translocation due to specific interactions with the tip of EF-G domain 4. Furthermore, EF-G accelerates ribosome rearrangements that restore the ribosome's control over the codon-anticodon interaction at the end of the movement. Our data explain how the mRNA reading frame is maintained during translation.