The Ribosome-bound Initiation Factor 2 Recruits Initiator TRNA to the 30S Initiation Complex
Overview
Authors
Affiliations
Bacterial translation initiation factor 2 (IF2) is a GTPase that promotes the binding of the initiator fMet-tRNA(fMet) to the 30S ribosomal subunit. It is often assumed that IF2 delivers fMet-tRNA(fMet) to the ribosome in a ternary complex, IF2.GTP.fMet-tRNA(fMet). By using rapid kinetic techniques, we show here that binding of IF2.GTP to the 30S ribosomal subunit precedes and is independent of fMet-tRNA(fMet) binding. The ternary complex formed in solution by IF2.GTP and fMet-tRNA is unstable and dissociates before IF2.GTP and, subsequently, fMet-tRNA(fMet) bind to the 30S subunit. Ribosome-bound IF2 might accelerate the recruitment of fMet-tRNA(fMet) to the 30S initiation complex by providing anchoring interactions or inducing a favourable ribosome conformation. The mechanism of action of IF2 seems to be different from that of tRNA carriers such as EF-Tu, SelB and eukaryotic initiation factor 2 (eIF2), instead resembling that of eIF5B, the eukaryotic subunit association factor.
Application of bio-layer interferometry for the analysis of ribosome-protein interactions.
Pandiarajan I, Walunj S, Banerjee N, Rout J, Srivastava S, Patankar S Front Mol Biosci. 2024; 11:1398964.
PMID: 39148630 PMC: 11325027. DOI: 10.3389/fmolb.2024.1398964.
Tuning tRNAs for improved translation.
Weiss J, Decker J, Bolano A, Krahn N Front Genet. 2024; 15:1436860.
PMID: 38983271 PMC: 11231383. DOI: 10.3389/fgene.2024.1436860.
Lamotrigine-mediated rescue of RsgA-deficient reveals another role of IF2 in ribosome biogenesis.
Singh S, Singh J, Varshney U J Bacteriol. 2024; 206(7):e0011924.
PMID: 38837341 PMC: 11270870. DOI: 10.1128/jb.00119-24.
Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.
Sigal M, Matsumoto S, Beattie A, Katoh T, Suga H Chem Rev. 2024; 124(10):6444-6500.
PMID: 38688034 PMC: 11122139. DOI: 10.1021/acs.chemrev.3c00894.
Soh W, Roetschke H, Cormican J, Teo B, Chiam N, Raabe M Nat Commun. 2024; 15(1):1147.
PMID: 38326304 PMC: 10850103. DOI: 10.1038/s41467-024-45339-3.