A specific monovalent metal ion integral to the AA platform of the RNA tetraloop receptor

Nat Struct Biol. 1998 Nov;5(11):986-92. doi: 10.1038/2960.


Metal ions are essential for the folding and activity of large catalytic RNAs. While divalent metal ions have been directly implicated in RNA tertiary structure formation, the role of monovalent ions has been largely unexplored. Here we report the first specific monovalent metal ion binding site within a catalytic RNA. As seen crystallographically, a potassium ion is coordinated immediately below AA platforms of the Tetrahymena ribozyme P4-P6 domain, including that within the tetraloop receptor. Interference and kinetic experiments demonstrate that potassium ion binding within the tetraloop receptor stabilizes the folding of the P4-P6 domain and enhances the activity of the Azoarcus group I intron. Since a monovalent ion binding site is integral to the tetraloop receptor, a tertiary structural motif that occurs frequently in RNA, monovalent metal ions are likely to participate in the folding and activity of a wide diversity of RNAs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenine / chemistry*
  • Animals
  • Binding Sites
  • Cations, Monovalent / chemistry*
  • Cesium / chemistry
  • Crystallography, X-Ray
  • Guanosine / analogs & derivatives
  • Guanosine / chemistry
  • Nucleic Acid Conformation*
  • Potassium / chemistry
  • RNA Splicing
  • RNA, Catalytic / chemistry*
  • RNA, Protozoan / chemistry
  • Tetrahymena
  • Thallium / chemistry
  • Thionucleosides / chemistry


  • Cations, Monovalent
  • RNA, Catalytic
  • RNA, Protozoan
  • Thionucleosides
  • Guanosine
  • Cesium
  • Thallium
  • 6-thioguanosine
  • Adenine
  • Potassium