Engineering a high-affinity methyl-CpG-binding protein
Details
Download: 16893950_BIB_B66C83CC4B5D.pdf (269.62 [Ko])
State: Public
Version: Final published version
License: CC BY-NC 4.0
State: Public
Version: Final published version
License: CC BY-NC 4.0
Serval ID
serval:BIB_B66C83CC4B5D
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
Engineering a high-affinity methyl-CpG-binding protein
Journal
Nucleic Acids Research
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Publication state
Published
Issued date
2006
Volume
34
Number
13
Pages
e96
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Publication Status: epublish
Abstract
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.
Keywords
DNA-Binding Proteins/chemistry, DNA-Binding Proteins/genetics, DNA-Binding Proteins/metabolism, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
13/07/2018 9:00
Last modification date
20/08/2019 15:24