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Inosine induces context-dependent recoding and translational stalling.

Konstantin Licht1, Markus Hartl2, Fabian Amman3

  • 1Center for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstrasse 17, A-1090 Vienna, Austria.

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|November 22, 2018
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Summary
This summary is machine-generated.

RNA modifications like inosine impact mRNA fate. This study reveals inosine can be read as guanosine, adenosine, or uracil by ribosomes, affecting translation and causing ribosome stalling.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Genetics

Background:

  • RNA modifications regulate gene expression by influencing mRNA processing, translation, and stability.
  • Inosine, a prevalent modification in metazoan mRNA, results from adenosine deamination by ADAR1 or ADAR2.
  • Inosine is generally presumed to be recognized as guanosine during cellular processes, including translation.

Purpose of the Study:

  • To systematically investigate the ribosomal decoding of inosine in mRNA.
  • To determine the fidelity and context-dependency of inosine interpretation by the ribosome.
  • To explore the impact of inosine on ribosome behavior and translational efficiency in vivo.

Main Methods:

  • Systematic testing of ribosomal decoding using mass spectrometry.
  • Analysis of ribosome profiling data from human tissues.
  • Mass spectrometry to detect inosine-mediated ribosome stalling.

Main Results:

  • Inosine is primarily decoded as guanosine, but can also be interpreted as adenosine and, rarely, uracil.
  • The decoding of inosine as adenosine or uracil is context-dependent.
  • Inosine induces ribosome stalling, particularly when multiple inosine modifications occur within a codon, which is confirmed in human tissues.

Conclusions:

  • This study provides the first comprehensive and unbiased assessment of inosine decoding by ribosomes.
  • Inosine exhibits novel and unexpected decoding patterns, expanding the coding potential of mRNA.
  • Inosine modifications significantly influence translational efficiency and introduce context-dependent variations in protein synthesis.