The X-linked methylated DNA binding protein, Mecp2, is subject to X inactivation in the mouse

1995 ◽  
Vol 6 (8) ◽  
pp. 491-492 ◽  
Author(s):  
D. A. Adler ◽  
N. A. Quaderi ◽  
S. D. M. Brown ◽  
V. M. Chapman ◽  
J. Moore ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
X Inactivation ◽  
Methylated Dna ◽  
Protein Mecp2

scholarly journals Multiple Modes of Interaction between the Methylated DNA Binding Protein MeCP2 and Chromatin

2006 ◽  
Vol 27 (3) ◽  
pp. 864-877 ◽  
Author(s):  
Tatiana Nikitina ◽  
Xi Shi ◽  
Rajarshi P. Ghosh ◽  
Rachel A. Horowitz-Scherer ◽  
Jeffrey C. Hansen ◽  
...  
Keyword(s):  
Dna Binding ◽  
Conformational Changes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Chromatin Interaction ◽  
Wild Type ◽  
Mobility Shift ◽  
Methylated Dna ◽  
Neurodevelopmental Disease ◽  
Protein Mecp2

ABSTRACT Mutations of the methylated DNA binding protein MeCP2, a multifunctional protein that is thought to transmit epigenetic information encoded as methylated CpG dinucleotides to the transcriptional machinery, give rise to the debilitating neurodevelopmental disease Rett syndrome (RTT). In this in vitro study, the methylation-dependent and -independent interactions of wild-type and mutant human MeCP2 with defined DNA and chromatin substrates were investigated. A combination of electrophoretic mobility shift assays and visualization by electron microscopy made it possible to understand the different conformational changes underlying the gel shifts. MeCP2 is shown to have, in addition to its well-established methylated DNA binding domain, a methylation-independent DNA binding site (or sites) in the first 294 residues, while the C-terminal portion of MeCP2 (residues 295 to 486) contains one or more essential chromatin interaction regions. All of the RTT-inducing mutants tested were quantitatively bound to chromatin under our conditions, but those that tend to be associated with the more severe RTT symptoms failed to induce the extensive compaction observed with wild-type MeCP2. Two modes of MeCP2-driven compaction were observed, one promoting nucleosome clustering and the other forming DNA-MeCP2-DNA complexes. MeCP2 binding to DNA and chromatin involves a number of different molecular interactions, some of which result in compaction and oligomerization. The multifunctional roles of MeCP2 may be reflected in these different interactions.

scholarly journals The major histocompatibility complex class II promoter-binding protein RFX (NF-X) is a methylated DNA-binding protein.

1993 ◽  
Vol 13 (11) ◽  
pp. 6810-6818 ◽  
Author(s):  
X Y Zhang ◽  
N Jabrane-Ferrat ◽  
C K Asiedu ◽  
S Samac ◽  
B M Peterlin ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Binding ◽  
Dna Sequences ◽  
Protein Complexes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Class Ii ◽  
Major Histocompatibility ◽  
Methylated Dna ◽  
Mammalian Protein

A mammalian protein called RFX or NF-X binds to the X box (or X1 box) in the promoters of a number of major histocompatibility (MHC) class II genes. In this study, RFX was shown to have the same DNA-binding specificity as methylated DNA-binding protein (MDBP), and its own cDNA was found to contain a binding site for MDBP in the leader region. MDBP is a ubiquitous mammalian protein that binds to certain DNA sequences preferentially when they are CpG methylated and to other related sequences, like the X box, irrespective of DNA methylation. MDBP from HeLa and Raji cells formed DNA-protein complexes with X-box oligonucleotides that coelectrophoresed with those containing standard MDBP sites. Furthermore, MDBP and X-box oligonucleotides cross-competed for the formation of these DNA-protein complexes. DNA-protein complexes obtained with MDBP sites displayed the same partial supershifting with an antiserum directed to the N terminus of RFX seen for complexes containing an X-box oligonucleotide. Also, the in vitro-transcribed-translated product of a recombinant RFX cDNA bound specifically to MDBP ligands and displayed the DNA methylation-dependent binding of MDBP. RFX therefore contains MDBP activity and thereby also EF-C, EP, and MIF activities that are indistinguishable from MDBP and that bind to methylation-independent sites in the transcriptional enhancers of polyomavirus and hepatitis B virus and to an intron of c-myc.

scholarly journals Effect of site-specific DNA methylation and mutagenesis on recognition by methylated DNA-binding protein from human placenta

1986 ◽  
Vol 14 (21) ◽  
pp. 8387-8397 ◽  
Author(s):  
Xian-Yang Zhang ◽  
Kenneth C. Ehrlich ◽  
Richard Y.-H. Wang ◽  
Melanie Ehrlich
Keyword(s):  
Dna Methylation ◽  
Dna Binding ◽  
Human Placenta ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Site Specific ◽  
Methylated Dna

scholarly journals Highly repeated sites in the apolipoprotein(a) gene recognized by methylated DNA-binding protein, a sequence-specific DNA-binding protein.

1990 ◽  
Vol 10 (9) ◽  
pp. 4957-4960 ◽  
Author(s):  
K C Ehrlich ◽  
M Ehrlich
Keyword(s):  
Risk Factor ◽  
Dna Binding ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein ◽  
High Plasma ◽  
Methylated Dna ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
Lower Molecular Mass

Methylated DNA-binding protein (MDBP), a sequence-specific DNA-binding protein, was found to recognize more than 30 sites within an allele of the human apolipoprotein(a) gene. High plasma levels of apolipoprotein(a), a risk factor for atherosclerosis, have been correlated with genetically inherited lower-molecular-mass isoforms of this protein. MDBP might help down modulate the expression of the apolipoprotein(a) gene in a manner dependent on the length of a given allele of the gene and the number of MDBP sites in it.

scholarly journals Methylated DNA-binding protein from human placenta recognizes specific methylated sites on several prokaryotic DNAs

1986 ◽  
Vol 14 (24) ◽  
pp. 9843-9860 ◽  
Author(s):  
Richard Y.H. Wang ◽  
Xian-Yang Zhang ◽  
Rana Khan ◽  
Youwen Zhou ◽  
Lan-Hsiang Huang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Human Placenta ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Methylated Dna
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