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  • Title: Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA.
    Author: Orr JW, Hagerman PJ, Williamson JR.
    Journal: J Mol Biol; 1998 Jan 23; 275(3):453-64. PubMed ID: 9466923.
    Abstract:
    The Bacillus stearothermophilus ribosomal protein S15 binds to the central domain of the 16 S rRNA inducing a conformational change in a three-way helical junction. To understand the nature of this conformational change, extended-helical junctions were prepared to examine the effects of S15 or Mg2+ binding on the relative helical orientation using native gel electrophoretic mobility and transient electric birefringence. The free junction is planar with approximately 120 degrees interhelical angles, whereas S15 and Mg2+ yield a junction conformation that remains planar in which two helices, 21 and 22, become colinear and the third, helix 20, forms a 60 degrees angle with respect to helix 22. This conformational change is thought to be important for directing the assembly of the central domain of the 30 S ribosomal subunit.
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