The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
Article Abstract:
MBD4, a mammalian protein that contains a methyl-CpG binding domain, has been found to efficiently remove thymine or uracil from a mismatched CpG site in vitro. The methyl-CpG binding domain of MBD4 binds preferentially to m5Cpg.TpG mismatches. It is suggested that this enzyme could act to minimize mutation at methyl-CpG. It is known that CpG to TpG transitions play an important role in genetic disease and cancer, and the impact of MBD4 loss on mutation frequency and cancer predisposition should therefore be investigated.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
Article Abstract:
Research shows that the methyl-CpG-binding nuclear protein MeCP2 collects at the transcriptional-repression domain together with the corepressor complex containing the transcriptional repressor mSin3A and histone deacetylases. Evidence indicates that MeCP2 gene regulation interacts with deoxyribonucleic acid methylation and histone deacetylation processes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Mutant weed breaks silence
Article Abstract:
A new study of mutated Arabidopsis plants shows that silencing and methylation of genes are not indissolubly linked.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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