RGD Reference Report - Structure-specific binding of MeCP2 to four-way junction DNA through its methyl CpG-binding domain. - Rat Genome Database

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Structure-specific binding of MeCP2 to four-way junction DNA through its methyl CpG-binding domain.

Authors: Galvao, TC  Thomas, JO 
Citation: Galvao TC and Thomas JO, Nucleic Acids Res. 2005 Nov 27;33(20):6603-9. Print 2005.
RGD ID: 1601323
Pubmed: PMID:16314321   (View Abstract at PubMed)
PMCID: PMC1298929   (View Article at PubMed Central)
DOI: DOI:10.1093/nar/gki971   (Journal Full-text)

MeCP2, whose methylated DNA-binding domain (MBD) binds preferentially to DNA containing 5Me-CpG relative to linear unmethylated DNA, also binds preferentially, and with similar affinity, to unmethylated four-way DNA junctions through the MBD. The Arg133Cys (R133C) mutation in the MBD, a Rett syndrome mutation that abolishes binding to methylated DNA, leads to only a slight reduction in the affinity of the MBD for four-way junctions, suggesting distinct but partially overlapping modes of binding to junction and methylated DNA. Binding to unmethylated DNA junctions is likely to involve a subset of the interactions that occur with methylated DNA. High-affinity, methylation-independent binding to four-way junctions is consistent with additional roles for MeCP2 in chromatin, beyond recognition of 5Me-CpG.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
double-stranded methylated DNA binding  IDA 1601323 RGD 
four-way junction DNA binding  IDA 1601323 RGD 
unmethylated CpG binding  IDA 1601323 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Mecp2  (methyl CpG binding protein 2)


Additional Information