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Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation

Iron(II) and 2-oxoglutarate (2OG)-dependent dioxygenases involved in histone and DNA/RNA demethylation convert the cosubstrate 2OG and oxygen to succinate and carbon dioxide, resulting in hydroxylation of the methyl group of the substrates and subsequent demethylation. Recent evidence has shown that...

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Autores principales: Dong, Cheng, Zhang, Heng, Xu, Chao, Arrowsmith, Cheryl H., Min, Jinrong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4224472/
https://www.ncbi.nlm.nih.gov/pubmed/25485134
http://dx.doi.org/10.1107/S2052252514020922
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author Dong, Cheng
Zhang, Heng
Xu, Chao
Arrowsmith, Cheryl H.
Min, Jinrong
author_facet Dong, Cheng
Zhang, Heng
Xu, Chao
Arrowsmith, Cheryl H.
Min, Jinrong
author_sort Dong, Cheng
collection PubMed
description Iron(II) and 2-oxoglutarate (2OG)-dependent dioxygenases involved in histone and DNA/RNA demethylation convert the cosubstrate 2OG and oxygen to succinate and carbon dioxide, resulting in hydroxylation of the methyl group of the substrates and subsequent demethylation. Recent evidence has shown that these 2OG dioxygenases play vital roles in a variety of biological processes, including transcriptional regulation and gene expression. In this review, the structure and function of these dioxygenases in histone and nucleic acid demethylation will be discussed. Given the important roles of these 2OG dioxygenases, detailed analysis and comparison of the 2OG dioxygenases will guide the design of target-specific small-molecule chemical probes and inhibitors.
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spelling pubmed-42244722014-12-05 Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation Dong, Cheng Zhang, Heng Xu, Chao Arrowsmith, Cheryl H. Min, Jinrong IUCrJ Feature Articles Iron(II) and 2-oxoglutarate (2OG)-dependent dioxygenases involved in histone and DNA/RNA demethylation convert the cosubstrate 2OG and oxygen to succinate and carbon dioxide, resulting in hydroxylation of the methyl group of the substrates and subsequent demethylation. Recent evidence has shown that these 2OG dioxygenases play vital roles in a variety of biological processes, including transcriptional regulation and gene expression. In this review, the structure and function of these dioxygenases in histone and nucleic acid demethylation will be discussed. Given the important roles of these 2OG dioxygenases, detailed analysis and comparison of the 2OG dioxygenases will guide the design of target-specific small-molecule chemical probes and inhibitors. International Union of Crystallography 2014-10-28 /pmc/articles/PMC4224472/ /pubmed/25485134 http://dx.doi.org/10.1107/S2052252514020922 Text en © Cheng Dong et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Feature Articles
Dong, Cheng
Zhang, Heng
Xu, Chao
Arrowsmith, Cheryl H.
Min, Jinrong
Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title_full Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title_fullStr Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title_full_unstemmed Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title_short Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation
title_sort structure and function of dioxygenases in histone demethylation and dna/rna demethylation
topic Feature Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4224472/
https://www.ncbi.nlm.nih.gov/pubmed/25485134
http://dx.doi.org/10.1107/S2052252514020922
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