JBC, Vol. 253, Issue 1, 18-20, Jan, 1978
Changes in the conformation and stability of 5 S RNA upon the binding of ribosomal proteins
J. W. Fox and K. P. Wong
The binding of ribosomal proteins L25, L18, and L5 to 5 S RNA results in a
conformational change and a destabilization of the 5 S RNA molecule. The
changes observed in the near ultraviolet circular dichroism (CD) spectra
and in the melting profiles indicate an increase in base stacking uith an
accompanying increase in asymmetry of the bases and a decrease in the
conformational stability of the 5 S RNA. These results are consistent with
the interpretation that the binding of these proteins increases the
stacking of specific single-stranded bases in 5 S RNA and aligns them in
helical arrays, resulting in a conformation which facilitates base-pairing
with nucleotide segment(s) of the ribosomal 23 S RNA or the transfer RNA
(or both). The simple and precise difference CD method described here is
potentially useful for studying subtle conformational changes of other
nucleic acid-protein interactions.