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

CW Greider, EH Blackburn - Cell, 1987 - cell.com
CW Greider, EH Blackburn
Cell, 1987cell.com
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 …
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.
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