LYRM protein

Leucine-Tyrosine-Arginine motif-containing proteins, also known as LYRM proteins or simply LYRMs, are a superfamily of small (11–22 kDa), basic, predominantly mitochondrial proteins found exclusively in eukaryotes and named after their conserved LYR-like motif near the N-terminus. They function as accessory subunits or assembly factors of OXPHOS complexes I, II, III and V and play essential roles in iron–sulfur (Fe–S) cluster biogenesis, mitochondrial translation, electron transfer flavoprotein (ETF) function, and acetate metabolism. Most LYRM proteins depend on mitochondrial fatty acid synthesis (mtFAS) for their function, as they are allosterically activated by binding to acylated mitochondrial acyl carrier protein (acyl-mtACP). It has been proposed that this mechanism evolved to protect cells from the toxic interactions between iron and oxygen.