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Cryo-EM reveals evolutionarily conserved and distinct structural features of plant CG maintenance methyltransferase MET1
by
Nishiyama, Atsuya
, To, Taiko Kim
, Kikuchi, Amika
, Arita, Kyohei
, Nakanishi, Makoto
, Chiba, Yoshie
in
101/28
/ 631/337/176/1988
/ 631/449/1659
/ 631/45/173
/ 631/535/1258/1259
/ 82/29
/ 82/83
/ Arabidopsis - enzymology
/ Arabidopsis - genetics
/ Arabidopsis - metabolism
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Arabidopsis Proteins - ultrastructure
/ Binding
/ Binding sites
/ Cryoelectron Microscopy
/ Deoxyribonucleic acid
/ DNA
/ DNA (Cytosine-5-)-Methyltransferase 1 - chemistry
/ DNA (Cytosine-5-)-Methyltransferase 1 - genetics
/ DNA (Cytosine-5-)-Methyltransferase 1 - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - chemistry
/ DNA (Cytosine-5-)-Methyltransferases - genetics
/ DNA (Cytosine-5-)-Methyltransferases - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - ultrastructure
/ DNA Methylation
/ DNA methyltransferase
/ DNA structure
/ DNA, Plant - metabolism
/ DNMT1 protein
/ Electron microscopy
/ Epigenetics
/ Evolution, Molecular
/ Histone H3
/ Histones
/ Histones - metabolism
/ Humanities and Social Sciences
/ Maintenance
/ Mammals
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Protein Binding
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Stem cells
/ Structural analysis
2025
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Cryo-EM reveals evolutionarily conserved and distinct structural features of plant CG maintenance methyltransferase MET1
by
Nishiyama, Atsuya
, To, Taiko Kim
, Kikuchi, Amika
, Arita, Kyohei
, Nakanishi, Makoto
, Chiba, Yoshie
in
101/28
/ 631/337/176/1988
/ 631/449/1659
/ 631/45/173
/ 631/535/1258/1259
/ 82/29
/ 82/83
/ Arabidopsis - enzymology
/ Arabidopsis - genetics
/ Arabidopsis - metabolism
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Arabidopsis Proteins - ultrastructure
/ Binding
/ Binding sites
/ Cryoelectron Microscopy
/ Deoxyribonucleic acid
/ DNA
/ DNA (Cytosine-5-)-Methyltransferase 1 - chemistry
/ DNA (Cytosine-5-)-Methyltransferase 1 - genetics
/ DNA (Cytosine-5-)-Methyltransferase 1 - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - chemistry
/ DNA (Cytosine-5-)-Methyltransferases - genetics
/ DNA (Cytosine-5-)-Methyltransferases - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - ultrastructure
/ DNA Methylation
/ DNA methyltransferase
/ DNA structure
/ DNA, Plant - metabolism
/ DNMT1 protein
/ Electron microscopy
/ Epigenetics
/ Evolution, Molecular
/ Histone H3
/ Histones
/ Histones - metabolism
/ Humanities and Social Sciences
/ Maintenance
/ Mammals
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Protein Binding
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Stem cells
/ Structural analysis
2025
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Cryo-EM reveals evolutionarily conserved and distinct structural features of plant CG maintenance methyltransferase MET1
by
Nishiyama, Atsuya
, To, Taiko Kim
, Kikuchi, Amika
, Arita, Kyohei
, Nakanishi, Makoto
, Chiba, Yoshie
in
101/28
/ 631/337/176/1988
/ 631/449/1659
/ 631/45/173
/ 631/535/1258/1259
/ 82/29
/ 82/83
/ Arabidopsis - enzymology
/ Arabidopsis - genetics
/ Arabidopsis - metabolism
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Arabidopsis Proteins - ultrastructure
/ Binding
/ Binding sites
/ Cryoelectron Microscopy
/ Deoxyribonucleic acid
/ DNA
/ DNA (Cytosine-5-)-Methyltransferase 1 - chemistry
/ DNA (Cytosine-5-)-Methyltransferase 1 - genetics
/ DNA (Cytosine-5-)-Methyltransferase 1 - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - chemistry
/ DNA (Cytosine-5-)-Methyltransferases - genetics
/ DNA (Cytosine-5-)-Methyltransferases - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - ultrastructure
/ DNA Methylation
/ DNA methyltransferase
/ DNA structure
/ DNA, Plant - metabolism
/ DNMT1 protein
/ Electron microscopy
/ Epigenetics
/ Evolution, Molecular
/ Histone H3
/ Histones
/ Histones - metabolism
/ Humanities and Social Sciences
/ Maintenance
/ Mammals
/ Models, Molecular
/ Molecular modelling
/ multidisciplinary
/ Protein Binding
/ Protein Domains
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Stem cells
/ Structural analysis
2025
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Cryo-EM reveals evolutionarily conserved and distinct structural features of plant CG maintenance methyltransferase MET1
Journal Article
Cryo-EM reveals evolutionarily conserved and distinct structural features of plant CG maintenance methyltransferase MET1
2025
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Overview
DNA methylation is essential for genomic function and transposable element silencing. In plants, DNA methylation occurs in CG, CHG, and CHH contexts (where H = A, T, or C), with the maintenance of CG methylation mediated by the DNA methyltransferase MET1. The molecular mechanism by which MET1 maintains CG methylation, however, remains unclear. Here, we report cryogenic electron microscopy structures of
Arabidopsis thaliana
MET1. We find that the methyltransferase domain of MET1 specifically methylates hemimethylated DNA in vitro. The structure of MET1 bound to hemimethylated DNA reveals the activation mechanism of MET1 resembling that of mammalian DNMT1. Curiously, the structure of apo-MET1 shows an autoinhibitory state distinct from that of DNMT1, where the RFTS2 domain and the connecting linker inhibit DNA binding. The autoinhibition of MET1 is relieved upon binding of a potential activator, ubiquitinated histone H3. Taken together, our structural analysis demonstrates both conserved and distinct molecular mechanisms regulating CG maintenance methylation in plant and animal DNA methyltransferases.
DNA methyltransferase MET1 maintains CG methylation in plants. Kikuchi determined the cryo-EM structure of
Arabidopsis
MET1, revealing autoinhibition and activation mechanisms, with conserved and plant-specific features distinct from mammalian DNMT1.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/29
/ 82/83
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Arabidopsis Proteins - ultrastructure
/ Binding
/ DNA
/ DNA (Cytosine-5-)-Methyltransferase 1 - chemistry
/ DNA (Cytosine-5-)-Methyltransferase 1 - genetics
/ DNA (Cytosine-5-)-Methyltransferase 1 - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - chemistry
/ DNA (Cytosine-5-)-Methyltransferases - genetics
/ DNA (Cytosine-5-)-Methyltransferases - metabolism
/ DNA (Cytosine-5-)-Methyltransferases - ultrastructure
/ Histones
/ Humanities and Social Sciences
/ Mammals
/ Proteins
/ Science
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