The ribosome-associated quality control pathway supports survival in the absence of non-stop ribosome rescue factors.

Unlabelled: In bacteria, if a ribosome translates an mRNA lacking a stop codon it becomes stalled at the 3' end of the message. These ribosomes must be rescued by -translation or the alternative rescue factors (ArfA or ArfB). However, mounting evidence suggests that the ribosome quality control (RQC) pathway may also rescue non-stop ribosomes.

YebC2 resolves ribosome stalling at polyprolines independent of EF-P and the ABCF ATPase YfmR.

Polyproline motifs are essential structural features of many proteins, and recent evidence suggests that EF-P is one of several factors that facilitate their translation. For example, YfmR was recently identified as a protein that prevents ribosome stalling at proline-containing sequences in the absence of EF-P. Here, we show that the YebC-family protein YebC2 (formerly YeeI) functions as a translation factor in that resolves ribosome stalling at polyprolines.

YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.

Protein synthesis is performed by the ribosome and a host of highly conserved elongation factors. Elongation factor P (EF-P) prevents ribosome stalling at difficult-to-translate sequences, such as polyproline tracts. In bacteria, phenotypes associated with deletion range from modest to lethal, suggesting that some species encode an additional translation factor that has similar function to EF-P.

YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.

Protein synthesis is performed by the ribosome and a host of highly conserved elongation factors. Elongation factor P (EF-P) prevents ribosome stalling at difficult-to-translate sequences, particularly polyproline tracts. In bacteria, phenotypes associated with deletion range from modest to lethal, suggesting that some species encode an additional translation factor that has similar function to EF-P.

Elongation Factor P Is Important for Sporulation Initiation.

The universally conserved protein elongation factor P (EF-P) facilitates translation at amino acids that form peptide bonds with low efficiency, particularly polyproline tracts. Despite its wide conservation, it is not essential in most bacteria and its physiological role remains unclear. Here, we show that EF-P affects the process of sporulation initiation in the bacterium Bacillus subtilis.