Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana.
Biomol NMR Assign
; 13(1): 59-62, 2019 04.
Article
in En
| MEDLINE
| ID: mdl-30242623
ABSTRACT
Epigenetic regulation is essential to various biological phenomena such as cell differentiation and cancer. DNA methylation is one of the most important epigenetic signals, as it is directly involved in gene silencing of transposable elements, genomic imprinting, and chromosome X inactivation. To mediate these processes, methyl-CpG-binding domain (MBD) proteins recognize specific signals encoded in the form of DNA methylation patterns. AtMBD6, one of the 12 MBD proteins in Arabidopsis thaliana, shares a high sequential homology in the MBD domain with mammalian MBD proteins, but a detailed characterization of its structural and functional properties remains elusive. Here, we report the 1H, 13C, and 15N resonance assignments of the isolated MBD domain of AtMBD6. Analysis of the chemical shift data implied that the MBD domain of AtMBD6 has a secondary structure similar to that of mammalian MeCP2, while the ß-strands ß1 and ß3 of AtMBD6 were found to be longer than those of MeCP2. The structural differences provide insight into the different recognition mechanisms of methylated DNA by plant and mammalian MBDs. The assignments reported here will aid further analyses such as titration experiments and three-dimensional structure determination using NMR to yield a detailed characterization of the interaction between AtMBD6 and methylated DNAs.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arabidopsis
/
Nuclear Magnetic Resonance, Biomolecular
/
Arabidopsis Proteins
/
DNA-Binding Proteins
Language:
En
Journal:
Biomol NMR Assign
Journal subject:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Year:
2019
Document type:
Article
Affiliation country:
Japan