RNA recognition and cleavage by a splicing endonuclease.

Publication Type:

Journal Article


Science, Volume 312, Issue 5775, p.906-10 (2006)


Amino Acid Sequence, Archaeal Proteins, Archaeoglobus fulgidus, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Dimerization, Endoribonucleases, Hydrogen Bonding, Introns, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Conformation, Protein Subunits, RNA Precursors, RNA Splicing, RNA, Archaeal, RNA, Transfer


<p>The RNA splicing endonuclease cleaves two phosphodiester bonds within folded precursor RNAs during intron removal, producing the functional RNAs required for protein synthesis. Here we describe at a resolution of 2.85 angstroms the structure of a splicing endonuclease from Archaeglobus fulgidus bound with a bulge-helix-bulge RNA containing a noncleaved and a cleaved splice site. The endonuclease dimer cooperatively recognized a flipped-out bulge base and stabilizes sharply bent bulge backbones that are poised for an in-line RNA cleavage reaction. Cooperativity arises because an arginine pair from one catalytic domain sandwiches a nucleobase within the bulge cleaved by the other catalytic domain.</p>