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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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Published in: | Proceedings of the National Academy of Sciences - PNAS 2005-07, Vol.102 (28), p.9778-9783 |
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container_end_page | 9783 |
container_issue | 28 |
container_start_page | 9778 |
container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Lue, N.F Bosoy, D Moriarty, T.J Autexier, C Altman, B Leng, S |
description | 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. |
doi_str_mv | 10.1073/pnas.0502252102 |
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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. 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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. 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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 |
title | Telomerase can act as a template- and RNA-independent terminal transferase |
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