scholarly journals The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus

1997 ◽  
Vol 25 (24) ◽  
pp. 5052-5056 ◽  
Author(s):  
S Schwarz
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Histone H1 ◽  
Methylated Dna ◽  
C Terminus

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

scholarly journals LIM Protein KyoT2 Negatively Regulates Transcription by Association with the RBP-J DNA-Binding Protein

1998 ◽  
Vol 18 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Yoshihito Taniguchi ◽  
Takahisa Furukawa ◽  
Tin Tun ◽  
Hua Han ◽  
Tasuku Honjo
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Negative Regulator ◽  
Nuclear Antigen ◽  
Differential Splicing ◽  
Barr Virus ◽  
Lim Domains ◽  
C Terminus

ABSTRACT The RBP-J/Su(H) DNA-binding protein plays a key role in transcriptional regulation by targeting Epstein-Barr virus nuclear antigen 2 (EBNA2) and the intracellular portions of Notch receptors to specific promoters. Using the yeast two-hybrid system, we isolated a LIM-only protein, KyoT, which physically interacts with RBP-J. Differential splicing gave rise to two transcripts of theKyoT gene, KyoT1 and KyoT2, that encoded proteins with four and two LIM domains, respectively. With differential splicing resulting in deletion of an exon, KyoT2 lacked two LIM domains from the C terminus and had a frameshift in the last exon, creating the RBP-J-binding region in the C terminus. KyoT1 had a negligible level of interaction with RBP-J. Strong expression of KyoT mRNAs was detected in skeletal muscle and lung, with a predominance of KyoT1 mRNA. When expressed in F9 embryonal carcinoma cells, KyoT1 and KyoT2 were localized in the cytoplasm and the nucleus, respectively. The binding site of KyoT2 on RBP-J overlaps those of EBNA2 and Notch1 but is distinct from that of Hairless, the negative regulator of RBP-J-mediated transcription in Drosophila. KyoT2 but not KyoT1 repressed the RBP-J-mediated transcriptional activation by EBNA2 and Notch1 by competing with them for binding to RBP-J and by dislocating RBP-J from DNA. KyoT2 is a novel negative regulatory molecule for RBP-J-mediated transcription in mammalian systems.

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 Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNA.

1997 ◽  
Vol 17 (4) ◽  
pp. 2194-2201 ◽  
Author(s):  
S D Miller ◽  
K Moses ◽  
L Jayaraman ◽  
C Prives
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Binding Protein ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Single Stranded Dna ◽  
C Terminus ◽  
P53 Response

Human replication protein A (RP-A) (also known as human single-stranded DNA binding protein, or HSSB) is a multisubunit complex involved in both DNA replication and repair. Potentially important to both these functions, it is also capable of complex formation with the tumor suppressor protein p53. Here we show that although p53 is unable to prevent RP-A from associating with a range of single-stranded DNAs in solution, RP-A is able to strongly inhibit p53 from functioning as a sequence-specific DNA binding protein when the two proteins are complexed. This inhibition, in turn, can be regulated by the presence of various lengths of single-stranded DNAs, as RP-A, when bound to these single-stranded DNAs, is unable to interact with p53. Interestingly, the lengths of single-stranded DNA capable of relieving complex formation between the two proteins represent forms that might be introduced through repair and replicative events. Increasing p53 concentrations can also overcome the inhibition by steady-state levels of RP-A, potentially mimicking cellular points of balance. Finally, it has been shown previously that p53 can itself be stimulated for site-specific DNA binding when complexed through the C terminus with short single strands of DNA, and here we show that p53 stays bound to these short strands even after binding a physiologically relevant site. These results identify a potential dual role for single-stranded DNA in the regulation of DNA binding by p53 and give insights into the p53 response to DNA damage.

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