The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex
2010 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Milon, Pohl ; Carotti, Marcello; Konevega, Andrey L. ; Wintermeyer, Wolfgang ; Rodnina, Marina V. ; Gualerzi, Claudio O.
- Abstract
- 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.
- Issue Date
- 2010
- Journal
- EMBO reports
- ISSN
- 1469-221X
- Language
- English