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Nascent polypeptide within the exit tunnel ensures continuous translation elongation by stabilizing the translating ribosome

View ORCID ProfileYuhei Chadani, Nobuyuki Sugata, Tatsuya Niwa, Yosuke Ito, Shintaro Iwasaki, View ORCID ProfileHideki Taguchi
doi: https://doi.org/10.1101/2021.02.02.429294
Yuhei Chadani
1Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan
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  • ORCID record for Yuhei Chadani
  • For correspondence: chadani.y.aa@m.titech.ac.jp taguchi@bio.titech.ac.jp
Nobuyuki Sugata
2School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8503, Japan
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Tatsuya Niwa
1Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan
2School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8503, Japan
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Yosuke Ito
2School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8503, Japan
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Shintaro Iwasaki
3RNA Systems Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Saitama, Japan
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Hideki Taguchi
1Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan
2School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, 226-8503, Japan
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  • For correspondence: chadani.y.aa@m.titech.ac.jp taguchi@bio.titech.ac.jp
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Summary

Continuous translation elongation, irrespective of amino acid sequences, is a prerequisite for living organisms to produce their proteomes. However, the risk of elongation abortion is concealed within nascent polypeptide products. Negatively charged sequences with occasional intermittent prolines, termed intrinsic ribosome destabilization (IRD) sequences, destabilizes the translating ribosomal complex. Thus, some nascent chain sequences lead to premature translation cessation. Here, we show that the risk of IRD is maximal at the N-terminal regions of proteins encoded by dozens of Escherichia coli genes. In contrast, most potential IRD sequences in the middle of open reading frames remain cryptic. We found two elements in nascent chains that counteract IRD: the nascent polypeptide itself that spans the exit tunnel and its bulky amino acid residues that occupy the tunnel entrance region. Thus, nascent polypeptide products have a built-in ability to ensure elongation continuity by serving as a bridge and thus by protecting the large and small ribosomal subunits from dissociation.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted February 02, 2021.
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Nascent polypeptide within the exit tunnel ensures continuous translation elongation by stabilizing the translating ribosome
Yuhei Chadani, Nobuyuki Sugata, Tatsuya Niwa, Yosuke Ito, Shintaro Iwasaki, Hideki Taguchi
bioRxiv 2021.02.02.429294; doi: https://doi.org/10.1101/2021.02.02.429294
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Nascent polypeptide within the exit tunnel ensures continuous translation elongation by stabilizing the translating ribosome
Yuhei Chadani, Nobuyuki Sugata, Tatsuya Niwa, Yosuke Ito, Shintaro Iwasaki, Hideki Taguchi
bioRxiv 2021.02.02.429294; doi: https://doi.org/10.1101/2021.02.02.429294

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