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Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB
Mutation patterns of DNA adducts, such as mutational spectra and signatures, are useful tools for diagnostic and prognostic purposes. Mutational spectra of carcinogens derive from three sources: adduct formation, replication bypass, and repair. Here, we consider the repair aspect of 1,N(6)-ethenoade...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8434105/ https://www.ncbi.nlm.nih.gov/pubmed/34500720 http://dx.doi.org/10.3390/molecules26175285 |
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author | Qi, Rui Bian, Ke Chen, Fangyi Tang, Qi Zhou, Xianhao Li, Deyu |
author_facet | Qi, Rui Bian, Ke Chen, Fangyi Tang, Qi Zhou, Xianhao Li, Deyu |
author_sort | Qi, Rui |
collection | PubMed |
description | Mutation patterns of DNA adducts, such as mutational spectra and signatures, are useful tools for diagnostic and prognostic purposes. Mutational spectra of carcinogens derive from three sources: adduct formation, replication bypass, and repair. Here, we consider the repair aspect of 1,N(6)-ethenoadenine (εA) by the 2-oxoglutarate/Fe(II)-dependent AlkB family enzymes. Specifically, we investigated εA repair across 16 possible sequence contexts (5′/3′ flanking base to εA varied as G/A/T/C). The results revealed that repair efficiency is altered according to sequence, enzyme, and strand context (ss- versus ds-DNA). The methods can be used to study other aspects of mutational spectra or other pathways of repair. |
format | Online Article Text |
id | pubmed-8434105 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84341052021-09-12 Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB Qi, Rui Bian, Ke Chen, Fangyi Tang, Qi Zhou, Xianhao Li, Deyu Molecules Brief Report Mutation patterns of DNA adducts, such as mutational spectra and signatures, are useful tools for diagnostic and prognostic purposes. Mutational spectra of carcinogens derive from three sources: adduct formation, replication bypass, and repair. Here, we consider the repair aspect of 1,N(6)-ethenoadenine (εA) by the 2-oxoglutarate/Fe(II)-dependent AlkB family enzymes. Specifically, we investigated εA repair across 16 possible sequence contexts (5′/3′ flanking base to εA varied as G/A/T/C). The results revealed that repair efficiency is altered according to sequence, enzyme, and strand context (ss- versus ds-DNA). The methods can be used to study other aspects of mutational spectra or other pathways of repair. MDPI 2021-08-31 /pmc/articles/PMC8434105/ /pubmed/34500720 http://dx.doi.org/10.3390/molecules26175285 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Brief Report Qi, Rui Bian, Ke Chen, Fangyi Tang, Qi Zhou, Xianhao Li, Deyu Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title | Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title_full | Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title_fullStr | Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title_full_unstemmed | Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title_short | Sequence Dependent Repair of 1,N(6)-Ethenoadenine by DNA Repair Enzymes ALKBH2, ALKBH3, and AlkB |
title_sort | sequence dependent repair of 1,n(6)-ethenoadenine by dna repair enzymes alkbh2, alkbh3, and alkb |
topic | Brief Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8434105/ https://www.ncbi.nlm.nih.gov/pubmed/34500720 http://dx.doi.org/10.3390/molecules26175285 |
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