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

Magnesium ions are abundant and play indispensable functions in the ribosome. A decrease in Mg<sup>2+</sup> concentration causes 70S ribosome dissociation and subsequent unfolding. Structural distortion at low Mg<sup>2+</sup> concentrations has been observed in an immature pr...

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Main Authors: Ting Yu, Junyi Jiang, Qianxi Yu, Xin Li, Fuxing Zeng
Format: Article
Language:English
Published: MDPI AG 2023-03-01
Series:Biomolecules
Subjects:
Online Access:https://www.mdpi.com/2218-273X/13/3/566
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author Ting Yu
Junyi Jiang
Qianxi Yu
Xin Li
Fuxing Zeng
author_facet Ting Yu
Junyi Jiang
Qianxi Yu
Xin Li
Fuxing Zeng
author_sort Ting Yu
collection DOAJ
description Magnesium ions are abundant and play indispensable functions in the ribosome. A decrease in Mg<sup>2+</sup> concentration causes 70S ribosome dissociation and subsequent unfolding. Structural distortion at low Mg<sup>2+</sup> 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 <i>E. coli</i> cells under various Mg<sup>2+</sup> concentrations and analyzed their structural distortion by cryo-electron microscopy. Upon systematically interrogating the structural heterogeneity within the 1 mM Mg<sup>2+</sup> 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 Mg<sup>2+</sup> 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. Mg<sup>2+</sup> 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 Mg<sup>2+</sup> in ribosomes suggests that the conformational changes reported here are likely shared due to a lack of cellular Mg<sup>2+</sup> in all domains of life.
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spelling doaj.art-cf6dc9bc49e34f02a0792111e3281ed42023-11-17T09:53:06ZengMDPI AGBiomolecules2218-273X2023-03-0113356610.3390/biom13030566Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium ConcentrationsTing Yu0Junyi Jiang1Qianxi Yu2Xin Li3Fuxing Zeng4Department of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, ChinaDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, ChinaDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, ChinaDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, ChinaDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, ChinaMagnesium ions are abundant and play indispensable functions in the ribosome. A decrease in Mg<sup>2+</sup> concentration causes 70S ribosome dissociation and subsequent unfolding. Structural distortion at low Mg<sup>2+</sup> 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 <i>E. coli</i> cells under various Mg<sup>2+</sup> concentrations and analyzed their structural distortion by cryo-electron microscopy. Upon systematically interrogating the structural heterogeneity within the 1 mM Mg<sup>2+</sup> 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 Mg<sup>2+</sup> 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. Mg<sup>2+</sup> 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 Mg<sup>2+</sup> in ribosomes suggests that the conformational changes reported here are likely shared due to a lack of cellular Mg<sup>2+</sup> in all domains of life.https://www.mdpi.com/2218-273X/13/3/566structural distortionmagnesium concentrationribosomeCryoEM
spellingShingle Ting Yu
Junyi Jiang
Qianxi Yu
Xin Li
Fuxing Zeng
Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
Biomolecules
structural distortion
magnesium concentration
ribosome
CryoEM
title Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
title_full Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
title_fullStr Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
title_full_unstemmed Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
title_short Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
title_sort structural insights into the distortion of the ribosomal small subunit at different magnesium concentrations
topic structural distortion
magnesium concentration
ribosome
CryoEM
url https://www.mdpi.com/2218-273X/13/3/566
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