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

TitleTelomerase can act as a template- and RNA-independent terminal transferase.
Publication TypeJournal Article
Year of Publication2005
AuthorsLue NF, Bosoy D, Moriarty TJ, Autexier C, Altman B, Leng S
JournalProc Natl Acad Sci U S A
Volume102
Issue28
Pagination9778-83
Date Published2005 Jul 12
ISSN0027-8424
KeywordsBase Sequence, DNA, DNA Primers, DNA Replication, Electrophoresis, Humans, Manganese, Reticulocytes, Saccharomyces cerevisiae, Telomerase, Telomere, Transferases
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.

DOI10.1073/pnas.0502252102
Alternate JournalProc Natl Acad Sci U S A
PubMed ID15994230
PubMed Central IDPMC1174988
Grant List54638 / / Canadian Institutes of Health Research / Canada
R01 GM062631 / GM / NIGMS NIH HHS / United States
GM 62631 / GM / NIGMS NIH HHS / United States

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