Key result
The N-terminal domain of IF2 promotes 70S initiation complex formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining.
The N-terminal domain of IF2 plays a critical role in stabilizing ribosomal subunit joining and proper tRNA positioning during translation initiation.
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No immediate clinical implications; leaves open IF2 domain targeting for future antibiotic development.
Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC, it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl(fMet)-tRNA(fMet) positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.
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Simonetti et al. (2013) studied this question. Deletion of IF2 N-terminal domain vs. Full-length IF2 was evaluated on 70S initiation complex formation and transpeptidation. The N-terminal domain of IF2 promotes 70S initiation complex formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining.
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