Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2

Opresko, P. L.

doi:10.1093/nar/gki273

Cited by 290Telomeres, Telomerase, and SenescenceDNA and Nucleic Acid ChemistryDNA Repair Mechanisms

Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2

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Opresko, P. L.·2005·Nucleic Acids Research

DOI 10.1093/nar/gki273PMC PMC549571

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Abstract

The ends of linear chromosomes are capped by protein-DNA complexes termed telomeres. Telomere repeat binding factors 1 and 2 (TRF1 and TRF2) bind specifically to duplex telomeric DNA and are critical components of functional telomeres. Consequences of telomere dysfunction include genomic instability, cellular apoptosis or senescence and organismal aging. Mild oxidative stress induces increased erosion and loss of telomeric DNA in human fibroblasts. We performed binding assays to determine whether oxidative DNA damage in telomeric DNA alters the binding activity of TRF1 and TRF2 proteins. Here, we report that a single 8-oxo-guanine lesion in a defined telomeric substrate reduced the percentage of bound TRF1 and TRF2 proteins by at least 50%, compared with undamaged telomeric DNA. More dramatic effects on TRF1 and TRF2 binding were observed with multiple 8-oxo-guanine lesions in the tandem telomeric repeats. Binding was likewise disrupted when certain intermediates of base excision repair were present within the telomeric tract, namely abasic sites or single nucleotide gaps. These studies indicate that oxidative DNA damage may exert deleterious effects on telomeres by disrupting the association of telomere-maintenance proteins TRF1 and TRF2.

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8-oxo-Gs accumulate at telomeres, where they inhibit telomerase and decrease binding of telomeric proteins, leading to disruption of telomere length and precluding maintenance of chromosomal-end capping.
“In addition, 8-oxo-Gs accumulate at telomeres, where they inhibit telomerase and decrease the binding of telomeric proteins, leading to the disruption of telomere length and precluding the maintenance of chromosomal-end capping46.”
From ROS in cancer therapy: the bright side of the moon (2020) · cites this paper as [46]
The Results and Discussion (page numbers unavailable) show that 8-oxoG lesions in defined telomeric DNA substrates reduce TRF1 and TRF2 binding. The paper does not show that 8-oxoG accumulates at telomeres or inhibits telomerase. It proposes possible effects on telomere function but says further studies are needed to establish the consequences for telomere structure and function; the claimed disruption of length and prevention of end capping are therefore not established. (LLM, conf=0.90)
Experimental — accuracy not yet measured
Oxidative stress induces tDD without telomere shortening and accelerates telomere shortening by inhibiting telomerase and disrupting recognition by telomere-binding proteins, contributing to uncapping.
“Oxidative stress reportedly both induces tDD without telomere shortening and accelerates telomere shortening23–26 by inhibiting telomerase27 and disrupting the recognition by telomere-binding proteins, which contributes to telomere uncapping22,28.”
From Telomere dysfunction in ageing and age-related diseases (2022) · cites this paper as [28]
Oxidative damage at telomeres displaces shelterin proteins TRF1 and TRF2.
“oxidative damage at telomeres displaces shelterin proteins TRF1 and TRF2, which might be another mechanism by which oxidative stress leads to telomere dysfunction (Opresko et al., 2005).”
From Telomeres and cell senescence—size matters not (2017) · cites this paper as Opresko et al., 2005

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doi:10.1093/nar/gki273 Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2
Opresko, P. L., Fan, J., Danzy, S., Wilson, D. M., III, & Bohr, V. A. (2005)
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Authors: Opresko, P. L.
Affiliations: National Institutes of Health (US)
Corresponding author: Opresko, P. L.
ORCID: Opresko, P. L.
Venue: Nucleic Acids Research
Publisher: Oxford University Press (OUP)
Published: 2005-02-23
Volume: 33
Issue: 4
Pages: 1230-1239
ISSN: 0305-1048 (ISSN-L)
1362-4962
DOI: 10.1093/nar/gki273
PMC: PMC549571
OpenAlex: W2098312065
Cited by: 289
References: 40
Citations by year: 2026: 10 · 2025: 15 · 2024: 10 · 2023: 17 · 2022: 19 · 2021: 20 · 2020: 23 · 2019: 18 · 2018: 15 · 2017: 14 · 2016: 20 · 2015: 20 · 2014: 17 · 2013: 14 · 2012: 6
FWCI: 4.61
Type: journal article
Language: en
Open access: gold
doi.org
Licence: other-oa
Locations: Nucleic Acids Research (publishedVersion, other-oa)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Institutes of Health
Topics: Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords: telomeres, TRF1, TRF2, oxidative DNA damage, 8-oxoguanine, telomeric DNA binding, base excision repair, abasic sites, telomere dysfunction, telomere shortening
MeSH terms: DNA, DNA Damage, Guanine, Humans, Telomere, Oxidative Stress, Telomeric Repeat Binding Protein 1, Telomeric Repeat Binding Protein 2

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Oxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2

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