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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Main Authors:	Wenjing Li, Tianlong Zhang, Mingliang Sun, Yu Shi, Xiao-Jie Zhang, Guo-Liang Xu, Jianping Ding
Format:	Article
Language:	English
Published:	Nature Publishing Group 2021-02-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-021-21061-2

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spelling	doaj-998b20601bc74f88a0e1304c7a59a6902021-02-07T12:13:01ZengNature Publishing GroupNature Communications2041-17232021-02-0112111310.1038/s41467-021-21061-2Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1Wenjing Li0Tianlong Zhang1Mingliang Sun2Yu Shi3Xiao-Jie Zhang4Guo-Liang Xu5Jianping Ding6State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of SciencesC5-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.https://doi.org/10.1038/s41467-021-21061-2
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Wenjing Li Tianlong Zhang Mingliang Sun Yu Shi Xiao-Jie Zhang Guo-Liang Xu Jianping Ding
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2021-02-01
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.
url	https://doi.org/10.1038/s41467-021-21061-2
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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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