A team of researchers from the Universities of Newcastle and Umeå has discovered that a ribosomal protein exhibits a remarkable evolutionary transformation, with its three-dimensional structure changing drastically while its sequence remains relatively conserved.
The protein, known as msL1/msL2, is found in ribosomes of parasitic microorganisms called microsporidia, and it is suggested to play a role in stabilizing the highly reduced protein synthesis machinery in these unique organisms.
“Despite its conserved sequence, msL1/msL2 adopts distinct folds in two different microsporidian species, Encephalitozoon cuniculi, and Vairimorpha necatrix. This structural divergence is particularly striking given that the two proteins share approximately 41% sequence similarity,” comments Léon Schierholz, one of the authors from Umeå University.