ArticleThe Journal of biological chemistry2008
The three methyl-CpG-binding domains of AtMBD7 control its subnuclear localization and mobility.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Gene regulatory mechanisms downstream of DNA methylation.Nature reviews. Genetics · 2026Review
- Roles of methyl-CpG-binding-domain (MBD) protiens in regulation of biological processes in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- Characterization of DNA methylation reader proteins inGenome research · 2024Article
- Genome-Wide Screening and Characterization of Methyl-CpG-Binding Domain (MBD) Proteins inCurrent issues in molecular biology · 2024Article
- Revealing cis- and trans-regulatory elements underlying nuclear distribution and function of the Arabidopsis histone H2B.8 variant.BMC plant biology · 2024Article
- Structural Insights into Methylated DNA Recognition by the Methyl-CpG Binding Domain of MBD6 fromACS omega · 2022Article
- Regulation of Active DNA Demethylation by a Methyl-CpG-Binding Domain Protein in Arabidopsis thaliana.PLoS genetics · 2015Article
- Methyl-CpG-binding domain protein MBD7 is required for active DNA demethylation in Arabidopsis.Plant physiology · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three methyl-CpG-binding domain (MBD) proteins in Arabidopsis, AtMBD5, AtMBD6, and AtMBD7, are functional in binding methylated CpG dinucleotides in vitro and localize to the highly CpG-methylated chromocenters in vivo. These proteins differ, however, in their subnuclear localization pattern; AtMBD5 and AtMBD6, each containing a single MBD motif, show preference for two perinucleolar chromocenters, whereas AtMBD7, a naturally occurring poly-MBD protein containing three MBD motifs, localizes to all chromocenters. Here we studied the significance of multiple MBD motifs for subnuclear localization and mobility in living cells. We found that the number of MBD motifs determines the subnuclear localization of the MBD protein. Furthermore, live kinetic experiments showed that AtMBD7-green fluorescent protein (GFP) has lower mobility than AtMBD5-GFP and AtMBD6-GFP, which is conferred by cooperative activity of its three MBD motifs. Thus, the number of MBD motifs appears to affect not only binding affinity and mobility within the nucleus, but also the subnuclear localization of the protein. Our results suggest that poly-MBD proteins can directly affect chromatin structure by inducing intra- and inter-chromatin compaction via bridging over multiple methylated CpG sites.
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