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2006
- doi: 10.1093/nar/gkl527
- issn: 0305-1048
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info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkl527
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info:eu-repo/semantics/altIdentifier/pmid/16893950
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info:eu-repo/semantics/altIdentifier/eissn/1362-4962
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info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_B66C83CC4B5D2
info:eu-repo/semantics/openAccess , CC BY-NC 4.0 , https://creativecommons.org/licenses/by-nc/4.0/
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H.F. Jørgensen et al., « Engineering a high-affinity methyl-CpG-binding protein », Serveur académique Lausannois, ID : 10.1093/nar/gkl527
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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.