NDLI: Telomerase can act as a template- and RNA-independent terminal transferase

Content Provider	PubMed Central
Author	Lue, Neal F. Dimitry, Bosoy Moriarty, Tara J. Chantal, Autexier Altman, Brian Leng, Siyang
Copyright Year	2005
Abstract	Telomerase is a special reverse transcriptase that extends one strand of the telomere repeat by using a template embedded in an RNA subunit. Like other polymerases, telomerase is believed to use a pair of divalent metal ions (coordinated by a triad of aspartic acid residues) for catalyzing nucleotide addition. Here we show that, in the presence of manganese, both yeast and human telomerase can switch to a template- and RNA-independent mode of DNA synthesis, acting in effect as a terminal transferase. Even as a terminal transferase, yeast telomerase retains a species-dependent preference for GT-rich, telomere-like DNA on the 5′ end of the substrate. The terminal transferase activity of telomerase may account for some of the hitherto unexplained effects of telomerase overexpression on cell physiology.
Related Links	http://dx.doi.org/10.1073/pnas.0502252102
Ending Page	9783
Page Count	6
Starting Page	9778
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	28
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-07-12
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Telomerase can act as a template- and RNA-independent terminal transferase