title: Enzymatic activity of the conserved core of a group I self-splicing intron.
abstract: Splicing of the Tetrahymena ribosomal intron was first studied by Cech et al., who subsequently demonstrated that the intron RNA catalyses its own excision from a primary transcript to yield mature ribosomal RNA. This intron shares several short conserved sequences and a common secondary structure with several other introns, some of which have also been shown to self-splice. Here I show that the conserved core of the Tetrahymena intron can act in trans to catalyse the sequence-specific cleavage and addition of guanosine to a separate RNA substrate.
mesh_terms: D000818:Animals; D001483:Base Sequence; D002872:Chromosome Deletion; D004262:DNA Restriction Enzymes / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D009690:Nucleic Acid Conformation; D012326:RNA Splicing; D012335:RNA, Ribosomal / Q000032:analysis; D013768:Tetrahymena / Q000235:genetics*
chemical_list: D012335:RNA, Ribosomal; D006160:Guanosine Triphosphate; D004262:DNA Restriction Enzymes; D008274:Magnesium