Conformational changes in 16S ribosomal RNA induced by 30S ribosomal subunit proteins from Escherichia coli

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Science  01 Dec 1978:
Vol. 202, Issue 4371, pp. 999-1001
DOI: 10.1126/science.362531


Laser light scattering has been used to evaluate conformational differences between free 16S RNA and several specific protein-16S RNA complexes. Proteins that interact strongly with the 16S RNA early in subunit assembly stabilize the RNA chain against unfolding in 1 mM Mg2+ and actually promote the formation of a more compact teriary structure in 20 mM Mg2+. A vital function of these proteins may therfore consist in altering the configuration of the RNA so that further assembly reactions can take place.

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