Ribosomal Protein bL27 Protects Translating Ribosomes from tmRNA-SmpB
Seerpatham, D.; Wanes, G.; Pathirage, C.; Cabrera, M.; Usoro, E.; Koutmou, K.; Dunham, C.; Whitford, P.; Keiler, K.
Show abstract
Bacterial ribosomal protein bL27 is universally conserved and its amino terminus is adjacent to the peptidyl transfer center, yet its role in translation remains unclear. Combining genetics, biochemistry and molecular dynamics, we show that bL27 has an unexpected role in preventing trans-translation, the bacterial ribosome rescue mechanism, from interfering with protein synthesis. Deletion of the bL27 gene causes a 10,000-fold decrease in viability and this defect is partially rescued by deletion of the gene encoding tmRNA, a critical molecule for trans-translation. Molecular dynamics simulations also indicate that bL27 can slow the movement of tmRNA on the ribosome. These data link trans-translation and bL27, and support a model in which the amino terminus of bL27 acts as a gatekeeper to prevent tmRNA from sterically interfering with tRNA on the ribosome.
Matching journals
The top 4 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Ribosomal RNA 2'-O-methylations regulate translation by impacting ribosome dynamics 97%
- Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation 96%
- Synonymous codon substitutions perturb co-translational protein folding in vivo and impair cell fitness 96%
Similar papers in this journal
Similar papers in this journal
- Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing 96%
- Residue-by-residue analysis of cotranslational membrane protein integration in vivo 94%
- A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S complex via an uAUG intermediate. 94%
Similar papers in this journal
- Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation 96%
- A non-canonical RNA-binding domain of the Fragile X protein, FMRP, elicits translational repression independent of mRNA G-quadruplexes 95%
- tRNA m1G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.