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

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.

authors

Lue NF,Bosoy D,Moriarty TJ,Autexier C,Altman B,Leng S

doi

10.1073/pnas.0502252102

keywords:

subject

Has Abstract

pub_date

2005-07-12 00:00:00

pages

9778-83

issue

28

eissn

0027-8424

issn

1091-6490

pii

0502252102

journal_volume

102

pub_type

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