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Conformational changes in the 16S rRNA induced by ribosomal proteins in the assembly process of the 30S E. coli subunit

Conference · · Plant Physiol., Suppl.; (United States)
OSTI ID:6736980
Conformational changes induced in the 16S rRNA by interactions with ribosomal proteins S4, S8, S15, S17, and S20, were monitored by scanning transmission electron microscopy (STEM) and CD spectroscopy with the aim to clarify the mechanism of rRNA folding during the ribosome assembly. The RNA-protein complexes were prepared by the standard reconstitution procedure and were dialyzed against 60mM KCl, 2mM Mg(OAc)/sub 2/, 10mM Hepes-KOH, pH 7.5. In most combinations the protein binding induced folding of the 16S rRNA into more compact forms evident from the values of radii of gyration, calculated from the mass distribution within the RNA-protein complexes. The most significant conformational changes were observed in the complex of 16S rRNA with proteins S4, S8 and S15. However, even these particles did not show structural similarity to the complete 30S subunits. The CD spectra and melting profiles of the 16S RNA-protein complexes imply a similar net content of ordered secondary structure of 16S RNA but differences in its distribution. These results indicate that interactions of 16S rRNA with five ribosomal proteins involved in the initial steps of ribosome subunit assembly induce conformational changes but not to the same extent as in the complete 30S subunit.
Research Organization:
Roche Institute of Molecular Biology, Nutley, NJ (USA)
OSTI ID:
6736980
Report Number(s):
CONF-870644-
Conference Information:
Journal Name: Plant Physiol., Suppl.; (United States) Journal Volume: 46:6
Country of Publication:
United States
Language:
English