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Keyword
- AFM1
- atomic force microscopy1
- atomic force microscopy (AFM)1
- base pairs1
- bps1
- CpG1
- cytosine-guanosine dinucleotide1
- DNA binding protein1
- DNA methylation1
- epigenetics1
- gene regulation1
- IDR1
- intrinsically disordered region1
- MBD1
- mCpG1
- mean square displacement1
- methyl-CpG-binding domain1
- methylated CpG1
- MSD1
- nucleosome remodeling and deacetylase complex1
- NuRD1
- SAv-QD1
- single-molecule biophysics1
- streptavidin-coated quantum dot1
Molecular Biophysics
1 Results
- Research ArticleOpen Access
Densely methylated DNA traps Methyl-CpG–binding domain protein 2 but permits free diffusion by Methyl-CpG–binding domain protein 3
Journal of Biological ChemistryVol. 298Issue 10102428Published online: August 26, 2022- Gage O. Leighton
- Elizabeth Marie Irvin
- Parminder Kaur
- Ming Liu
- Changjiang You
- Dhruv Bhattaram
- and others
Cited in Scopus: 0The methyl-CpG–binding domain 2 and 3 proteins (MBD2 and MBD3) provide structural and DNA-binding function for the Nucleosome Remodeling and Deacetylase (NuRD) complex. The two proteins form distinct NuRD complexes and show different binding affinity and selectivity for methylated DNA. Previous studies have shown that MBD2 binds with high affinity and selectivity for a single methylated CpG dinucleotide while MBD3 does not. However, the NuRD complex functions in regions of the genome that contain many CpG dinucleotides (CpG islands).