Solution Structure of a Substrate for the Archaeal Pre-tRNA Splicing Endonucleases: The Bulge-Helix-Bulge Motif

• Published in: Molecular cell Vol. 1; no. 6; pp. 883 - 894
• Main Authors: Diener, John L, Moore, Peter B
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01-05-1998
• Subjects: 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; Space life sciences
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(00)80087-8

The structure of the bulge-helix-bulge motif that constitutes the intron/exon splice site in
H. volcanii pre-tRNA
Trp 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.