The telomere terminal transferase of tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity

Carol W. Greider, Elizabeth H. Blackburn

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)887-898
Number of pages12
JournalCell
Volume51
Issue number6
DOIs
StatePublished - Dec 24 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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