The telomere terminal transferase of Tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity
Language: 
English
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.

Author(s): 
Greider, C. W.
Blackburn, E. H.
Item Type: 
Journal Article
Publication Title: 
Cell
Journal Abbreviation: 
Cell
Publication Date: 
12/24/1987
Publication Year: 
1987
Pages: 
887-898
Volume: 
51
Issue: 
6
ISSN: 
0092-8674
Library Catalog: 
NCBI Published Medical (?)
Extra: 
PMID: 3319189

Turabian/Chicago Citation

C. W. Greider and E. H. Blackburn. 12/24/1987. "The telomere terminal transferase of Tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity." Cell 51: 6: 887-898.

Wikipedia Citation

<ref> {{Cite journal | doi = | issn = 0092-8674 | volume = 51 | pages = 887-898 | last = Greider | first = C. W. | coauthors = Blackburn, E. H. | title = The telomere terminal transferase of Tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity | journal = Cell | date = 12/24/1987 | pmid = | pmc = }} </ref>