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<p>The ribosome employs a set of highly conserved translation factors to efficiently synthesise proteins. Some translation factors interact with the ribosome in a transient manner and are thus challenging to identify. However, proteins involved in translation can be specifically identified by their interaction with ribosomal RNAs. Using a combination of proteomics approaches, we identified 30 previously uncharacterized RNA-binding proteins in the pathogenic bacterium <i>Streptococcus pyogenes</i>. One of these, a widely conserved protein YebC, was shown to transiently interact with 23S rRNA near the peptidyl-transferase centre. Deletion of <i>yebC</i> moderately affected the physiology and virulence of <i>S. pyogenes</i>. We performed ribosome profiling and detected increased pausing at proline-rich amino acid motifs in the absence of functional YebC. Further experiments in <i>S. pyogenes</i> and <i>Salmonella</i> Typhimurium and using an in vitro translation system suggested that YebC is a translation factor required for efficient translation of proteins with proline-rich motifs.</p>

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RNA-binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年7月7日

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  • Dmitriy Ignatov,
  • Vivekanandan Shanmuganathan,
  • Rina Ahmed-Begrich,
  • Kathirvel Alagesan,
  • Karin Hahnke,
  • Chu Wang,
  • Kathrin Krause,
  • Fabián A. Cornejo,
  • Kristin Funke,
  • Marc Erhardt,
  • Christian Karl Frese,
  • Emmanuelle Charpentier

摘要

The ribosome employs a set of highly conserved translation factors to efficiently synthesise proteins. Some translation factors interact with the ribosome in a transient manner and are thus challenging to identify. However, proteins involved in translation can be specifically identified by their interaction with ribosomal RNAs. Using a combination of proteomics approaches, we identified 30 previously uncharacterized RNA-binding proteins in the pathogenic bacterium Streptococcus pyogenes. One of these, a widely conserved protein YebC, was shown to transiently interact with 23S rRNA near the peptidyl-transferase centre. Deletion of yebC moderately affected the physiology and virulence of S. pyogenes. We performed ribosome profiling and detected increased pausing at proline-rich amino acid motifs in the absence of functional YebC. Further experiments in S. pyogenes and Salmonella Typhimurium and using an in vitro translation system suggested that YebC is a translation factor required for efficient translation of proteins with proline-rich motifs.