Abstract
The Bacillus stearothermophilus ribosomal protein S15 binds to the central domain of the 16 S rRNA inducing a conformational change in a threeway 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 ~120°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°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.
Original language | English (US) |
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Pages (from-to) | 453-464 |
Number of pages | 12 |
Journal | Journal of Molecular Biology |
Volume | 275 |
Issue number | 3 |
DOIs | |
State | Published - Jan 23 1998 |
Externally published | Yes |
Keywords
- 16 S ribosomal RNA
- Gel mobility shift
- Ribosomal protein S15
- RNA:protein interactions
- Transient electric birefringence
ASJC Scopus subject areas
- Virology