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

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 and Emmanuelle Charpentier ()
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Dmitriy Ignatov: Max Planck Unit for the Science of Pathogens
Vivekanandan Shanmuganathan: Max Planck Unit for the Science of Pathogens
Rina Ahmed-Begrich: Max Planck Unit for the Science of Pathogens
Kathirvel Alagesan: Max Planck Unit for the Science of Pathogens
Karin Hahnke: Max Planck Unit for the Science of Pathogens
Chu Wang: Max Planck Unit for the Science of Pathogens
Kathrin Krause: Max Planck Unit for the Science of Pathogens
Fabián A. Cornejo: Max Planck Unit for the Science of Pathogens
Kristin Funke: Humboldt-Universität zu Berlin
Marc Erhardt: Max Planck Unit for the Science of Pathogens
Christian Karl Frese: Max Planck Unit for the Science of Pathogens
Emmanuelle Charpentier: Max Planck Unit for the Science of Pathogens

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract 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.

Date: 2025
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DOI: 10.1038/s41467-025-60687-4

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