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

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 nucleotid...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2005-07, Vol.102 (28), p.9778-9783
Main Authors: Lue, N.F, Bosoy, D, Moriarty, T.J, Autexier, C, Altman, B, Leng, S
Format: Article
Language:English
Subjects:
Base Sequence
Biochemistry
Biological Sciences
DNA
DNA - genetics
DNA - metabolism
DNA Primers
DNA replication
DNA Replication - physiology
Electrophoresis
enzyme activity
Enzymes
Humans
Manganese
Manganese - metabolism
Metal ions
Nucleic acids
Nucleotides
Reticulocytes - metabolism
Ribonucleic acid
RNA
Saccharomyces cerevisiae
telomerase
Telomerase - metabolism
Telomere - genetics
Telomeres
terminal transferase
Transferases - metabolism
Yeasts
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0502252102