ArticleNature communications2025
RNA-binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Systems-level analysis predicts no autotrophy-linked protein-RNA interactions in Clostridium autoethanogenum.Nature communications · 2026Article
- Enhancing ribosomal translation of backbone-altering nonproteinogenic amino acids via YebC and YeeN.Nucleic acids research · 2026Article
- Functional redundancy of translation-associated factors masks the role of YebC2 in Enterococcus faecalis.Folia microbiologica · 2026Article
- Structure determination and dual targeting of a plant TACO1 identifies its ancient role as an organelle translation regulator.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of TACO1-mediated efficient mitochondrial translation.Nature communications · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025Article
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- YebC2 resolves ribosome stalling and increases fitness of cells lacking EF-P and the ABCF ATPase YfmR.PLoS genetics · 2025Article
- EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.Nature communications · 2024Article
- YebC2 resolves ribosome stalling at polyprolines independent of EF-P and the ABCF ATPase YfmR.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
12 authors.
Funding
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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