Engineering a high-affinity methyl-CpG-binding protein

Détails

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Etat: Public
Version: Final published version
Licence: CC BY-NC 4.0
ID Serval
serval:BIB_B66C83CC4B5D
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Institution
Titre
Engineering a high-affinity methyl-CpG-binding protein
Périodique
Nucleic Acids Research
Auteur(s)
Jørgensen H.F., Adie K., Chaubert P., Bird A.P.
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Statut éditorial
Publié
Date de publication
2006
Volume
34
Numéro
13
Pages
e96
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Résumé
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.
Mots-clé
DNA-Binding Proteins/chemistry, DNA-Binding Proteins/genetics, DNA-Binding Proteins/metabolism, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
13/07/2018 10:00
Dernière modification de la notice
20/08/2019 16:24
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