Abstract / Description of output
Core members of the MBD protein family (MeCP2, MBD1, MBD2 and MBD4) share a methyl-CpG-binding domain that has a specific affinity for methylated CpG sites in double-stranded DNA. By multimerizing the MDB domain of Mbd1, we engineered a poly-MBD protein that displays methyl-CpG-specific binding in vitro with a dissociation constant that is >50-fold higher than that of a monomeric MBD. Poly-MBD proteins also localize to methylated foci in cells and can deliver a functional domain to reporter constructs in vivo. We propose that poly-MBD proteins are sensitive reagents for the detection of DNA methylation levels in isolated native DNA and for cytological detection of chromosomal CpG methylation.
Original language | English |
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Pages (from-to) | e96 |
Journal | Nucleic Acids Research |
Volume | 34 |
Issue number | 13 |
DOIs | |
Publication status | Published - 2006 |
Keywords / Materials (for Non-textual outputs)
- Animals
- Cell Line
- CpG Islands
- DNA Methylation
- DNA-Binding Proteins
- Indicators and Reagents
- Mice
- Protein Engineering
- Protein Structure, Tertiary
- Recombinant Proteins