title: A conserved secondary structure for telomerase RNA.
abstract: The RNA moiety of the ribonucleoprotein enzyme telomerase contains the template for telomeric DNA synthesis. We present a secondary structure model for telomerase RNA, derived by a phylogenetic comparative analysis of telomerase RNAs from seven tetrahymenine ciliates. The telomerase RNA genes from Tetrahymena malaccensis, T. pyriformis, T. hyperangularis, T. pigmentosa, T. hegewishii, and Glaucoma chattoni were cloned, sequenced, and compared with the previously cloned RNA gene from T. thermophila and with each other. To define secondary structures of these RNAs, homologous complementary sequences were identified by the occurrence of covariation among putative base pairs. Although their primary sequences have diverged rapidly overall, a strikingly conserved secondary structure was identified for all these telomerase RNAs. Short regions of nucleotide conservation include a block of 22 totally conserved nucleotides that contains the telomeric templating region.
authors.affiliation: Department of Microbiology and Immunology, University of California, San Francisco 94143.
authors.forename: D P
authors.initials: DP
authors.lastname: Romero
authors.forename: E H
authors.initials: EH
authors.lastname: Blackburn
mesh_terms: D000818:Animals; D001482:Base Composition / Q000235:genetics; D001483:Base Sequence; D015139:Blotting, Southern; D016798:Ciliophora / Q000201:enzymology / Q000235:genetics; D003001:Cloning, Molecular; D004253:DNA Nucleotidylexotransferase / Q000737:chemistry* / Q000235:genetics; D014644:Genetic Variation / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016133:Polymerase Chain Reaction; D015138:RNA, Nuclear / Q000737:chemistry* / Q000235:genetics; D012261:Ribonucleoproteins / Q000737:chemistry*; D016415:Sequence Alignment; D013768:Tetrahymena / Q000201:enzymology* / Q000235:genetics
chemical_list: D015138:RNA, Nuclear; D012261:Ribonucleoproteins; D004253:DNA Nucleotidylexotransferase