Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif

Mol Cell. 1998 May;1(6):883-94.

Abstract

The structure of the bulge-helix-bulge motif that constitutes the intron/exon splice site in H. volcanii pre-tRNATrp has been determined by NMR spectroscopy. The conformations of the two 3 nt bulges, where the pre-tRNA is cleaved, are stabilized by stacking interactions between bulge nucleotides and bases in the adjacent Watson-Crick helices and by a network of backbone hydrogen bonds. Both bulges are presented on the same minor groove face of the central 4 bp helix, and the overall structure has approximate two-fold symmetry, which makes it well-suited for attack by archaeal splicing endonucleases, which are symmetric dimers.

Publication types

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

MeSH terms

  • Archaeal Proteins / analysis
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics*
  • Endoribonucleases / analysis
  • Endoribonucleases / chemistry
  • Endoribonucleases / metabolism*
  • Haloferax volcanii / enzymology
  • Haloferax volcanii / genetics*
  • Magnetic Resonance Spectroscopy
  • Nucleic Acid Conformation
  • Protein Structure, Tertiary
  • RNA Precursors / analysis
  • RNA Precursors / chemistry
  • RNA Precursors / genetics*
  • RNA Splicing / physiology*
  • RNA, Archaeal / chemistry
  • RNA, Archaeal / metabolism

Substances

  • Archaeal Proteins
  • RNA Precursors
  • RNA, Archaeal
  • Endoribonucleases