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Differential stability of E. coli ribosomal particles and free RNA towards thermal degradation studied by microcalorimetry

1998; Elsevier BV; Volume: 75; Issue: 2 Linguagem: Inglês

10.1016/s0301-4622(98)00197-5

1873-4200

A. Bonincontro, Stefania Cinelli, Marco Mengoni, G. Onori, Gianfranco Risuleo, A. Santucci,

RNA and protein synthesis mechanisms

We investigated the thermal degradation of E. coli ribosomes by differential scanning microcalorimetry. The 70S particles show two distinctive and irreversible peaks upon thermal degradation. Free rRNA in solution produces, on the contrary, an unstructured denaturation profile. The thermal analysis of 50S particles shows a profile substantially identical to that observed in 70S, while 30S particles produce an unstructured denaturation pattern. Therefore the thermal behavior of the 70S particle is essentially attributable to the denaturation of the 50S subunit. Our data validate previous observations that the 50S has a more rigid structure as compared to 30S, which behaves as a 'floppy' particle. In addition our data suggest that protein/RNA interactions play a significant role to stabilize three-dimensional structures of the ribosome.