Unfolding of E. coli ribosomes: evidence for pre-existing breaks in the large subunit.

An investigation has been made on structure modifications of E. coli ribosomes following EDTA treatment. When completely deprived of magnesium, the small subunit sediments at 16S while the large one, in the same conditions, shows two components at 17S and 21S. Unfolding causes in both subunits an increase in radius of gyration without substantial change in molecular weight, as shown by light scattering measurements. The occurence of the slower 17S component besides the 21S one has to be connected with a fraction of the large subunit population which presents nucleolytic breaks in its RNA chain. These breaks do not cause fragmentation of the unfolded subunit but lead to a more open configuration sedimenting at lower velocity.