Oxidative guanine base damage regulates human telomerase activity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-12

AUTHORS

Elise Fouquerel, Justin Lormand, Arindam Bose, Hui-Ting Lee, Grace S Kim, Jianfeng Li, Robert W Sobol, Bret D Freudenthal, Sua Myong, Patricia L Opresko

ABSTRACT

Changes in telomere length are associated with degenerative diseases and cancer. Oxidative stress and DNA damage have been linked to both positive and negative alterations in telomere length and integrity. Here we examined how the common oxidative lesion 8-oxo-7,8-dihydro-2'-deoxyguanine (8-oxoG) regulates telomere elongation by human telomerase. When 8-oxoG is present in the dNTP pool as 8-oxodGTP, telomerase utilization of the oxidized nucleotide during telomere extension is mutagenic and terminates further elongation. Depletion of MTH1, the enzyme that removes oxidized dNTPs, increases telomere dysfunction and cell death in telomerase-positive cancer cells with shortened telomeres. In contrast, a preexisting 8-oxoG within the telomeric DNA sequence promotes telomerase activity by destabilizing the G-quadruplex DNA structure. We show that the mechanism by which 8-oxoG arises in telomeres, either by insertion of oxidized nucleotides or by direct reaction with free radicals, dictates whether telomerase is inhibited or stimulated and thereby mediates the biological outcome. More... »

PAGES

1092-1100

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb.3319

    DOI

    http://dx.doi.org/10.1038/nsmb.3319

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1017106715

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/27820808


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