Inside the folded ribosomal RNA, at the interface where the two subunits meet, and on the ATP that activates every amino acid before it is added to the chain: those are the places in translation where magnesium sits, and that is where Howlithico starts.
Browse the tablesBacterial ribosomes are roughly two-thirds RNA; human ones are a little over half. Every nucleotide in that RNA carries a negatively charged phosphate group, so tightly packed stretches would push each other apart if positively charged counterparts were not present. Of those counterparts, the doubly charged magnesium ion is the one described most often.
In high-resolution structures, magnesium ions turn up where RNA helices crowd close together. Some ions attach directly to oxygen atoms of the phosphate groups; others keep their shell of water molecules and hold the chain in shape through hydrogen bonds.
The two parts of a ribosome touch at only a limited number of contact points. At several of them, RNA segments from both sides meet and are linked through bound ions. When the magnesium concentration in a test-tube setup drops, the ribosomes come apart into their two pieces.
Before an amino acid enters the chain, an enzyme attaches it to its tRNA. The first partial step is driven by ATP, which sits in the active site as a complex with magnesium. The ion lines up the phosphate groups so the amino acid can attack the inner phosphorus atom.
Sentence fixed in EU law
“Magnesium contributes to normal protein synthesis”
EU-authorized wording · Regulation (EU) No 432/2012
A ribosomal RNA is a long chain of thousands of nucleotides that folds into loops, double strands and dense knots. Because each phosphate group carries a negative charge, this folding needs partners that neutralize charge. Monovalent ions such as potassium do that too, but a magnesium ion packs twice the charge into a small space and can bridge two neighboring phosphates at once.
As early as the late 1950s, Alfred Tissières and James Watson noticed in ribosomes from gut bacteria that the complete particles split into two unequally sized parts when the buffer was low in magnesium, and joined up again when the level was raised. Today’s crystal and cryo-electron microscopy structures of bacterial ribosomes assign a magnesium ion to several hundred positions.
Each of the twenty standard amino acids has an enzyme of its own, an aminoacyl-tRNA synthetase. In the first partial step, the amino acid reacts with ATP; this yields a reactive intermediate, the aminoacyl adenylate, and releases pyrophosphate. In the second partial step, the amino acid moves from that intermediate onto the end of its tRNA. Magnesium takes part in the first step: it binds to the two outer phosphate groups of ATP and stabilizes the transition state of the reaction.
None of this appears in EU law apart from one single sentence for magnesium: “Magnesium contributes to normal protein synthesis” — EU-authorized wording · Regulation (EU) No 432/2012.
The wording names a contribution to the ordinary process in people who get enough of the mineral. It does not say how much protein a body makes, gives no dose and promises nothing about mood, sleep or appearance. Ribosomes, tRNA and synthetases explain why researchers looked into the link; they are not part of the authorized text.
The document gathers the tables from this website and adds structural sketches of the ribosomal subunits, a list of the human cytosolic synthetases with their enzyme class, and annotated original papers.
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