A novel 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 could be specifically identified by their interaction with ribosomal RNAs. In this study, we searched for novel RNA binding proteins in the pathogenic bacterium Streptococcus pyogenes. A combination of proteomics approaches identified several proteins of unknown function that interact with RNA. One of these, a universally conserved protein YebC, was shown to transiently interact with 23S rRNA near the peptidyl-transferase. The deletion of YebC moderately affected physiology and virulence of S. pyogenes. Site-directed mutagenesis in S. pyogenes identified several amino acids essential for YebC activity. We performed ribosome profiling and detected increased pausing at proline-rich amino acid stretches in the absence of functional YebC. Further results obtained with in vivo reporters and in vitro translation system suggest that YebC can alleviate ribosome stalling at polyproline stretches. In conclusion, our study shows that YebC is a novel translation factor required for efficient translation of proteins with proline-rich motifs.

INSTRUMENT(S):

ORGANISM(S): Streptococcus Pyogenes M1 Gas

SUBMITTER: Kathirvel Alagesan  

LAB HEAD: Emmanuelle Charpentier

PROVIDER: PXD054642 | Pride | 2025-07-14

REPOSITORIES: Pride