RNA-binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria
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...
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| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-60687-4 |
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| Summary: | 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. |
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| ISSN: | 2041-1723 |