Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1

C5-glyceryl-methylcytosine is a DNA modification that plays a role in the regulation of green alga photosynthesis and is catalysed by CMD1, using vitamin C (VC) as a co-substrate. Here, the authors provide insights into the catalytic mechanism of CMD1 by determining the crystal structures of apo CMD...

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Autores principales:	Wenjing Li, Tianlong Zhang, Mingliang Sun, Yu Shi, Xiao-Jie Zhang, Guo-Liang Xu, Jianping Ding
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/998b20601bc74f88a0e1304c7a59a690
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id	oai:doaj.org-article:998b20601bc74f88a0e1304c7a59a690
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spelling	oai:doaj.org-article:998b20601bc74f88a0e1304c7a59a6902021-12-02T14:06:16ZMolecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD110.1038/s41467-021-21061-22041-1723https://doaj.org/article/998b20601bc74f88a0e1304c7a59a6902021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21061-2https://doaj.org/toc/2041-1723C5-glyceryl-methylcytosine is a DNA modification that plays a role in the regulation of green alga photosynthesis and is catalysed by CMD1, using vitamin C (VC) as a co-substrate. Here, the authors provide insights into the catalytic mechanism of CMD1 by determining the crystal structures of apo CMD1 and CMD1 bound to either VC or DNA, as well as the ternary CMD1/VC/DNA complex structure.Wenjing LiTianlong ZhangMingliang SunYu ShiXiao-Jie ZhangGuo-Liang XuJianping DingNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Wenjing Li Tianlong Zhang Mingliang Sun Yu Shi Xiao-Jie Zhang Guo-Liang Xu Jianping Ding Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
description	C5-glyceryl-methylcytosine is a DNA modification that plays a role in the regulation of green alga photosynthesis and is catalysed by CMD1, using vitamin C (VC) as a co-substrate. Here, the authors provide insights into the catalytic mechanism of CMD1 by determining the crystal structures of apo CMD1 and CMD1 bound to either VC or DNA, as well as the ternary CMD1/VC/DNA complex structure.
format	article
author	Wenjing Li Tianlong Zhang Mingliang Sun Yu Shi Xiao-Jie Zhang Guo-Liang Xu Jianping Ding
author_facet	Wenjing Li Tianlong Zhang Mingliang Sun Yu Shi Xiao-Jie Zhang Guo-Liang Xu Jianping Ding
author_sort	Wenjing Li
title	Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
title_short	Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
title_full	Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
title_fullStr	Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
title_full_unstemmed	Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1
title_sort	molecular mechanism for vitamin c-derived c5-glyceryl-methylcytosine dna modification catalyzed by algal tet homologue cmd1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/998b20601bc74f88a0e1304c7a59a690
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Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1

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