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Journal Article

Conditional switch between frameshifting regimes upon translation of dnaX mRNA.

MPS-Authors
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Caliskan,  N.
Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Wohlgemuth,  I.
Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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

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

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Supplementary Material (public)

2444988_Suppl_1.pdf
(Supplementary material), 433KB

2444988_Suppl_2.xlsx
(Supplementary material), 19KB

2444988_Suppl_3.pdf
(Supplementary material), 4MB

Citation

Caliskan, N., Wohlgemuth, I., Korniy, N., Pearson, M., Peske, F., & Rodnina, M. V. (2017). Conditional switch between frameshifting regimes upon translation of dnaX mRNA. Molecular Cell, 66(4), 558-567. doi:10.1016/j.molcel.2017.04.023.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-4C95-4
Abstract
Ribosome frameshifting during translation of bacterial dnaX can proceed via different routes, generating a variety of distinct polypeptides. Using kinetic experiments, we show that -1 frameshifting predominantly occurs during translocation of two tRNAs bound to the slippery sequence codons. This pathway depends on a stem-loop mRNA structure downstream of the slippery sequence and operates when aminoacyl-tRNAs are abundant. However, when aminoacyl-tRNAs are in short supply, the ribosome switches to an alternative frameshifting pathway that is independent of a stem-loop. Ribosome stalling at a vacant 0-frame A-site codon results in slippage of the P-site peptidyl-tRNA, allowing for -1-frame decoding. When the -1-frame aminoacyl-tRNA is lacking, the ribosomes switch into -2 frame. Quantitative mass spectrometry shows that the -2-frame product is synthesized in vivo. We suggest that switching between frameshifting routes may enrich gene expression at conditions of aminoacyl-tRNA limitation.