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