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

Published version
Peer-reviewed

Type

Article

Change log

Authors

Galvao, TC 
Thomas, JO 

Abstract

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.

Description

Keywords

Amino Acid Sequence, Animals, Binding Sites, CpG Islands, DNA, DNA Methylation, Methyl-CpG-Binding Protein 2, Molecular Sequence Data, Protein Structure, Tertiary, Rats

Journal Title

Nucleic Acids Research

Conference Name

Journal ISSN

0305-1048
1362-4962

Volume Title

33

Publisher

Oxford University Press

Rights

Publisher's own licence