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DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity
Numerous studies have shown that select DNA repair enzyme activities impact response and/or toxicity of genotoxins, suggesting a requirement for enzyme functional analyses to bolster precision medicine or prevention. To address this need, we developed a DNA Repair Molecular Beacon (DRMB) platform th...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6114979/ https://www.ncbi.nlm.nih.gov/pubmed/30167090 http://dx.doi.org/10.18632/oncotarget.25859 |
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author | Li, Jianfeng Svilar, David McClellan, Steven Kim, Jung-Hyun Ahn, Eun-Young Erin Vens, Conchita Wilson, David M. Sobol, Robert W. |
author_facet | Li, Jianfeng Svilar, David McClellan, Steven Kim, Jung-Hyun Ahn, Eun-Young Erin Vens, Conchita Wilson, David M. Sobol, Robert W. |
author_sort | Li, Jianfeng |
collection | PubMed |
description | Numerous studies have shown that select DNA repair enzyme activities impact response and/or toxicity of genotoxins, suggesting a requirement for enzyme functional analyses to bolster precision medicine or prevention. To address this need, we developed a DNA Repair Molecular Beacon (DRMB) platform that rapidly measures DNA repair enzyme activity in real-time. The DRMB assay is applicable for discovery of DNA repair enzyme inhibitors, for the quantification of enzyme rates and is sufficiently sensitive to differentiate cellular enzymatic activity that stems from variation in expression or effects of amino acid substitutions. We show activity measures of several different base excision repair (BER) enzymes, including proteins with tumor-identified point mutations, revealing lesion-, lesion-context- and cell-type-specific repair dependence; suggesting application for DNA repair capacity analysis of tumors. DRMB measurements using lysates from isogenic control and APE1-deficient human cells suggests the major mechanism of base lesion removal by most DNA glycosylases may be mono-functional base hydrolysis. In addition, development of a microbead-conjugated DRMB assay amenable to flow cytometric analysis further advances its application. Our studies establish an analytical platform capable of evaluating the enzyme activity of select DNA repair proteins in an effort to design and guide inhibitor development and precision cancer therapy options. |
format | Online Article Text |
id | pubmed-6114979 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-61149792018-08-30 DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity Li, Jianfeng Svilar, David McClellan, Steven Kim, Jung-Hyun Ahn, Eun-Young Erin Vens, Conchita Wilson, David M. Sobol, Robert W. Oncotarget Research Paper Numerous studies have shown that select DNA repair enzyme activities impact response and/or toxicity of genotoxins, suggesting a requirement for enzyme functional analyses to bolster precision medicine or prevention. To address this need, we developed a DNA Repair Molecular Beacon (DRMB) platform that rapidly measures DNA repair enzyme activity in real-time. The DRMB assay is applicable for discovery of DNA repair enzyme inhibitors, for the quantification of enzyme rates and is sufficiently sensitive to differentiate cellular enzymatic activity that stems from variation in expression or effects of amino acid substitutions. We show activity measures of several different base excision repair (BER) enzymes, including proteins with tumor-identified point mutations, revealing lesion-, lesion-context- and cell-type-specific repair dependence; suggesting application for DNA repair capacity analysis of tumors. DRMB measurements using lysates from isogenic control and APE1-deficient human cells suggests the major mechanism of base lesion removal by most DNA glycosylases may be mono-functional base hydrolysis. In addition, development of a microbead-conjugated DRMB assay amenable to flow cytometric analysis further advances its application. Our studies establish an analytical platform capable of evaluating the enzyme activity of select DNA repair proteins in an effort to design and guide inhibitor development and precision cancer therapy options. Impact Journals LLC 2018-08-03 /pmc/articles/PMC6114979/ /pubmed/30167090 http://dx.doi.org/10.18632/oncotarget.25859 Text en Copyright: © 2018 Li et al. http://creativecommons.org/licenses/by/3.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) (CC-BY), which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Research Paper Li, Jianfeng Svilar, David McClellan, Steven Kim, Jung-Hyun Ahn, Eun-Young Erin Vens, Conchita Wilson, David M. Sobol, Robert W. DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title | DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title_full | DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title_fullStr | DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title_full_unstemmed | DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title_short | DNA Repair Molecular Beacon assay: a platform for real-time functional analysis of cellular DNA repair capacity |
title_sort | dna repair molecular beacon assay: a platform for real-time functional analysis of cellular dna repair capacity |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6114979/ https://www.ncbi.nlm.nih.gov/pubmed/30167090 http://dx.doi.org/10.18632/oncotarget.25859 |
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