Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif.
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.
Diener
J L
JL
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
Moore
P B
PB
D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D004722:Endoribonucleases / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D019622:Haloferax volcanii / Q000201:enzymology / Q000235:genetics*; D009682:Magnetic Resonance Spectroscopy; D009690:Nucleic Acid Conformation; D017434:Protein Structure, Tertiary; D012322:RNA Precursors / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D012326:RNA Splicing / Q000502:physiology*; D019642:RNA, Archaeal / Q000737:chemistry / Q000378:metabolism
D019843:Archaeal Proteins; D012322:RNA Precursors; D019642:RNA, Archaeal; D004722:Endoribonucleases