MBD4 is a DNA glycosylase that recognises and removes mismatched bases in DNA repair. Similarly to other proteins in the MBD family, MBD4 can recognise 5mCG/CG complexes, however, it is unique as it can also recognise and excise the mismatched thymine base in 5mCG/TG. MBD4 has been associated with DNA demethylation, which is important as DNA methylation plays a significant role in epigenetic modifications, including gene repression, imprinting and carcinogenesis. The presentation highlights the structural features of MBD4 that allow for its versatile base recognition, as found in the Otani et al. (2013) study.
References Otani, J., Arita, K., Kato, T., Kinoshita, M., Kimura, H., Suetake, I., Shirakawa, M. (2013). Structural basis of the versatile DNA recognition ability of the methyl-CpG binding domain of methyl-CpG binding domain protein 4. J Biol Chem, 288(9), 6351-6362. https://doi.org/10.1074/jbc.M112.431098
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