ArticleNucleic acids research2014
Solution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Exploring the bistable equilibrium of methylated CpG DNA recognition by the MBD2 protein.Nucleic acids research · 2026Article
- Mechanistic model for epigenetic maintenance by methyl-CpG-binding domain proteins.bioRxiv : the preprint server for biology · 2024Article
- Multi-omic analyses of m5C readers reveal their characteristics and immunotherapeutic proficiency.Scientific reports · 2024Article
- SRSF2 plays an unexpected role as reader of mMolecular cell · 2023Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- Structural Insights into Methylated DNA Recognition by the Methyl-CpG Binding Domain of MBD6 fromACS omega · 2022Article
- Proteins That Read DNA Methylation.Advances in experimental medicine and biology · 2022Article
- The Methyl-CpG-Binding Domain 2 and 3 Proteins and Formation of the Nucleosome Remodeling and Deacetylase Complex.Journal of molecular biology · 2020Review
- 5-methylcytosine promotes pathogenesis of bladder cancer through stabilizing mRNAs.Nature cell biology · 2019Article
- Web 3DNA 2.0 for the analysis, visualization, and modeling of 3D nucleic acid structures.Nucleic acids research · 2019Article
- NMR-based investigations into target DNA search processes of proteins.Methods (San Diego, Calif.) · 2018Review
- CH···O Hydrogen Bonds Mediate Highly Specific Recognition of Methylated CpG Sites by the Zinc Finger Protein Kaiso.Biochemistry · 2018Article
- Readers of DNA methylation, the MBD family as potential therapeutic targets.Pharmacology & therapeutics · 2018Review
- CpG and methylation-dependent DNA binding and dynamics of the methylcytosine binding domain 2 protein at the single-molecule level.Nucleic acids research · 2017Article
- Structural Basis of MeCP2 Distribution on Non-CpG Methylated and Hydroxymethylated DNA.Journal of molecular biology · 2017Article
- Methylation specific targeting of a chromatin remodeling complex from sponges to humans.Scientific reports · 2017Article
- Binding Analysis of Methyl-CpG Binding Domain of MeCP2 and Rett Syndrome Mutations.ACS chemical biology · 2016Article
- Role of base excision repair in maintaining the genetic and epigenetic integrity of CpG sites.DNA repair · 2015Review
- An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex.Nucleic acids research · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Unlike other members of the methyl-cytosine binding domain (MBD) family, MBD4 serves as a potent DNA glycosylase in DNA mismatch repair specifically targeting mCpG/TpG mismatches arising from spontaneous deamination of methyl-cytosine. The protein contains an N-terminal MBD (MBD4MBD) and a C-terminal glycosylase domain (MBD4GD) separated by a long linker. This arrangement suggests that the MBD4MBD either directly augments enzymatic catalysis by the MBD4GD or targets the protein to regions enriched for mCpG/TpG mismatches. Here we present structural and dynamic studies of MBD4MBD bound to dsDNA. We show that MBD4MBD binds with a modest preference for mCpG as compared to mismatch, unmethylated and hydroxymethylated DNA. We find that while MBD4MBD exhibits slow exchange between molecules of DNA (intermolecular exchange), the domain exhibits fast exchange between two sites in the same molecule of dsDNA (intramolecular exchange). Introducing a single-strand defect between binding sites does not greatly reduce the intramolecular exchange rate, consistent with a local hopping mechanism for moving along the DNA. These results support a model in which the MBD4MBD4 targets the intact protein to (m)CpG islands and promotes scanning by rapidly exchanging between successive mCpG sites which facilitates repair of nearby mCpG/TpG mismatches by the glycosylase domain.
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