Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA

Human thymine DNA glycosylase (hTDG) efficiently excises 5-carboxylcytosine (5caC), a key oxidation product of 5-methylcytosine in a recently discovered cytosine demethylation pathway. We present here the crystal structures of hTDG catalytic domain in complex with duplex DNA containing either 5caC o...

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Autores principales: Zhang, Liang, Lu, Xingyu, Lu, Junyan, Liang, Haihua, Dai, Qing, Xu, Guo-Liang, Luo, Cheng, Jiang, Hualiang, He, Chuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3307914/
https://www.ncbi.nlm.nih.gov/pubmed/22327402
http://dx.doi.org/10.1038/nchembio.914
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author Zhang, Liang
Lu, Xingyu
Lu, Junyan
Liang, Haihua
Dai, Qing
Xu, Guo-Liang
Luo, Cheng
Jiang, Hualiang
He, Chuan
author_facet Zhang, Liang
Lu, Xingyu
Lu, Junyan
Liang, Haihua
Dai, Qing
Xu, Guo-Liang
Luo, Cheng
Jiang, Hualiang
He, Chuan
author_sort Zhang, Liang
collection PubMed
description Human thymine DNA glycosylase (hTDG) efficiently excises 5-carboxylcytosine (5caC), a key oxidation product of 5-methylcytosine in a recently discovered cytosine demethylation pathway. We present here the crystal structures of hTDG catalytic domain in complex with duplex DNA containing either 5caC or a fluorinated analog. These structures, together with biochemical and computational analyses, reveal that 5caC is specifically recognized in the active site of hTDG, supporting the role of TDG in mammalian 5-methylcytosine (5mC) demethylation.
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spelling pubmed-33079142012-10-01 Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA Zhang, Liang Lu, Xingyu Lu, Junyan Liang, Haihua Dai, Qing Xu, Guo-Liang Luo, Cheng Jiang, Hualiang He, Chuan Nat Chem Biol Article Human thymine DNA glycosylase (hTDG) efficiently excises 5-carboxylcytosine (5caC), a key oxidation product of 5-methylcytosine in a recently discovered cytosine demethylation pathway. We present here the crystal structures of hTDG catalytic domain in complex with duplex DNA containing either 5caC or a fluorinated analog. These structures, together with biochemical and computational analyses, reveal that 5caC is specifically recognized in the active site of hTDG, supporting the role of TDG in mammalian 5-methylcytosine (5mC) demethylation. 2012-02-12 /pmc/articles/PMC3307914/ /pubmed/22327402 http://dx.doi.org/10.1038/nchembio.914 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Zhang, Liang
Lu, Xingyu
Lu, Junyan
Liang, Haihua
Dai, Qing
Xu, Guo-Liang
Luo, Cheng
Jiang, Hualiang
He, Chuan
Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title_full Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title_fullStr Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title_full_unstemmed Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title_short Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
title_sort thymine dna glycosylase specifically recognizes 5-carboxylcytosine-modified dna
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3307914/
https://www.ncbi.nlm.nih.gov/pubmed/22327402
http://dx.doi.org/10.1038/nchembio.914
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