4.7 Article

Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations

Journal

BIOMOLECULES
Volume 13, Issue 3, Pages -

Publisher

MDPI
DOI: 10.3390/biom13030566

Keywords

structural distortion; magnesium concentration; ribosome; CryoEM

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Magnesium ions are abundant and crucial in the ribosome, and a decrease in its concentration leads to ribosome dissociation and structural distortion. This study focused on the structural distortion of the 30S subunit under different magnesium concentrations. The decoding center and h17 were found to be significantly distorted, and the requirement for magnesium ions suggests that these conformational changes may be shared across all domains of life due to magnesium deficiency.
Magnesium ions are abundant and play indispensable functions in the ribosome. A decrease in Mg2+ concentration causes 70S ribosome dissociation and subsequent unfolding. Structural distortion at low Mg2+ concentrations has been observed in an immature pre50S, while the structural changes in mature subunits have not yet been studied. Here, we purified the 30S subunits of E. coli cells under various Mg2+ concentrations and analyzed their structural distortion by cryo-electron microscopy. Upon systematically interrogating the structural heterogeneity within the 1 mM Mg2+ dataset, we observed 30S particles with different levels of structural distortion in the decoding center, h17, and the 30S head. Our model showed that, when the Mg2+ concentration decreases, the decoding center distorts, starting from h44 and followed by the shifting of h18 and h27, as well as the dissociation of ribosomal protein S12. Mg2+ deficiency also eliminates the interactions between h17, h10, h15, and S16, resulting in the movement of h17 towards the tip of h6. More flexible structures were observed in the 30S head and platform, showing high variability in these regions. In summary, the structures resolved here showed several prominent distortion events in the decoding center and h17. The requirement for Mg2+ in ribosomes suggests that the conformational changes reported here are likely shared due to a lack of cellular Mg2+ in all domains of life.

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