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The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences

The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences

Proceedings of the National Academy of Sciences of the United States of America 89(20): 9499-9503

ISSN/ISBN: 0027-8424

PMID: 1409659

DOI: 10.2307/2360428

MDBP-2 is a repressor that binds preferentially to methylated DNA. Peptides derived from MDBP-2 were sequenced. The sequences of the two peptides, KPAGPS-VTELITK and ALAAGGYDVEK, are identical to those found in the chicken histone H1 core protein. In SDS/polyacrylamide gels MDBP-2 has an apparent molecular mass of 21 kDa, and antibodies directed against calf thymus total histone H1 cross-react with MDBP-2. The preferential binding of affinity-purified MDBP-2 to methylated DNA is not sequence-specific but requires a minimum length of 30 base pairs and one pair of symmetrically methylated (i.e., methylated on both strands) CpG dinucleotides. As previously shown, there is a decrease in the binding activity of MDBP-2 to methylated DNA upon estradiol treatment. Immunoblots show that upon estradiol treatment the amount of immunocrossreacting MDBP-2 protein remains unchanged. MDBP-2 enables another protein to bind DNA which by itself does not bind methylated DNA. Ultraviolet crosslinking and selective immunoadsorption assays with anti-histone H1 antibodies show that in vivo MDBP-2 preferentially binds to the methylated repressed vitellogenin gene. It is concluded that MDBP-2 may participate in the long-term silencing of genes (formation of heterochromatin) through selective binding to methylated DNA.

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Accession: 018177647

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