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

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.