The Telomere Terminal Transferase of Tetrahymena Is a Ribonucleoprotein Enzyme With Two Kinds of Primer Specificity

Cell. 1987 Dec 24;51(6):887-98. doi: 10.1016/0092-8674(87)90576-9.

Abstract

We have analyzed the de novo telomere synthesis catalyzed by the enzyme telomere terminal transferase (telomerase) from Tetrahymena. Oligonucleotides representing the G-rich strand of telomeric sequences from five different organisms specifically primed the addition of TTGGGG repeats in vitro, suggesting that primer recognition may involve a DNA structure unique to these oligonucleotides. The sequence at the 3' end of the oligonucleotide primer specified the first nucleotide added in the reaction. Furthermore, the telomerase was shown to be a ribonucleoprotein complex whose RNA and protein components were both essential for activity. After extensive purification of the enzyme by a series of five different chromatographic steps, a few small low abundance RNAs copurified with the activity.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chromosomes / metabolism
  • DNA / metabolism*
  • DNA Nucleotidylexotransferase / metabolism*
  • DNA Nucleotidyltransferases / metabolism*
  • Molecular Weight
  • Oligodeoxyribonucleotides / metabolism*
  • RNA, Catalytic
  • RNA, Ribosomal / metabolism
  • Repetitive Sequences, Nucleic Acid*
  • Ribonucleoproteins / metabolism*
  • Tetrahymena / enzymology*

Substances

  • Oligodeoxyribonucleotides
  • RNA, Catalytic
  • RNA, Ribosomal
  • Ribonucleoproteins
  • DNA
  • DNA Nucleotidyltransferases
  • DNA Nucleotidylexotransferase