Protein and Mg2+-induced conformational changes in the S15 binding site of 16 S ribosomal RNA

Jeffrey W. Orr, Paul J Hagerman, James R. Williamson

Research output: Contribution to journalArticlepeer-review

76 Scopus citations


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 languageEnglish (US)
Pages (from-to)453-464
Number of pages12
JournalJournal of Molecular Biology
Issue number3
StatePublished - Jan 23 1998
Externally publishedYes


  • 16 S ribosomal RNA
  • Gel mobility shift
  • Ribosomal protein S15
  • RNA:protein interactions
  • Transient electric birefringence

ASJC Scopus subject areas

  • Virology


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