Magnesium (Mg2+) is pivotal for the vitality, yield, and quality of horticultural crops. Central to plant physiology, Mg2+ powers photosynthesis as an integral component of chlorophyll, bolstering growth and biomass accumulation. Beyond basic growth, it critically affects crop quality factors, from chlorophyll synthesis to taste, texture, and shelf life. However, Mg2 + deficiency can cripple yields and impede plant development. Magnesium Transporters (MGTs) orchestrate Mg2+ dynamics, with notable variations observed in horticultural species such as Cucumis sativus, Citrullus lanatus, and Citrus sinensis. Furthermore, Mg2+ is key in fortifying plants against environmental stressors and diseases by reinforcing cell walls and spurring the synthesis of defense substances. A burgeoning area of research is the application of magnesium oxide nanoparticles (MgO-NPs), which, owing to their nanoscale size and high reactivity, optimize nutrient uptake, and enhance plant growth and stress resilience. Concurrently, modern breeding techniques provide insights into Mg2+ dynamics to develop crops with improved Mg2+ efficiency and resilience to deficiency. Effective Mg2+ management through soil tests, balanced fertilization, and pH adjustments holds promise for maximizing crop health, productivity, and sustainability. This review unravels the nuanced intricacies of Mg2+ in plant physiology and genetics, and its interplay with external factors, serving as a cornerstone for those keen on harnessing its potential for horticultural excellence.

The power of magnesium: unlocking the potential for increased yield, quality, and stress tolerance of horticultural crops

The importance of Mg2+ ions for RNA structure and function can difficultly be overstated. Several attempts were made to establish a comprehensive Mg2+ binding site classification. However, such descriptions were hampered by poorly modelled ion binding sites. Recently, ribosome cryo-EM structures with resolutions < 2.0 Å allowed more detailed ion binding site descriptions. However, such a task is challenging. In a recent 1.55 Å E. coli ribosome structure (PDBid 8B0X), ion assignment incompleteness/errors were observed that prevent a full understanding of the chelated ion structures. We reinspected this cryo-EM reconstruction by using stereochemical constraints derived from an updated analysis of the Mg2+/K+ occurrences in the Cambridge Structural Database (CSD) and established sufficiently straightforward and general binding principles to be applicable to any RNA of sufficient resolution. Through our improved characterization of the RNA ionic structure, we assigned all Mg2+ ions bound to 2 up to 4 non-water oxygens leading to a better understanding of the role of Mg2+ ions in folding while shedding light on the importance of Mg2+…Mg2+/K+ ion pairs in catalytic systems. Based on these data, we defined general Mg2+ binding rules allowing to describe unanticipated motifs where up to five adjacent nucleotides wrap around a single ion.

Principles of ion binding to RNA inferred from the analysis of a 1.55 Å resolution bacterial ribosome structure – Part I: Mg2+

The study is focused on the technology for surface modification of AZ31 magnesium alloy for biomedical applications, in particular in implantology. The experimental procedure consists of intentional stages that involve chemical treatment in piranha solution, plasma chemical activation of the alloy surface using Ar and O2 as gaseous precursors, and biopolymer coatings deposition—based on polylactic acid (PLA) and poly(lactic-co-glycolic acid) (PLGA) with the addition of caffeic acid—utilizing the immersion method. In the course of the experiment, the validity of the investigated technology of surface modification of AZ31 magnesium alloy was confirmed. The pre-treatment step guaranteed obtaining a higher surface roughness, resulting in homogeneous and stable biopolymer coatings with proper adhesion to the substrate. Moreover, the corrosion studies conducted confirmed better corrosion behaviour of the modified samples in SBF corrosive medium, and no significant release of the alloy-related ions was observed. Furthermore, the biopolymer coatings ensured non-cytotoxicity towards the MG-63 cell line and promoted cell proliferation with proper morphology. Based on the obtained results, it may be concluded that the proposed technology can be treated as an interesting and promising surface-engineering strategy for implantology and biodegradable materials applications. 

Surface Modification of AZ31 Mg Alloy Based on PLA or PLGA with Caffeic Acid for Bioengineering Applications

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.

/pdf/structural-insights-into-the-distortion-of-the-ribosomal-2mdo13xu.pdf

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

An alternative pathway for 50S assembly in the absence of functional DbpA.

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

An alternative pathway for 50S assembly in the absence of functional DbpA.