Abstract
The methylation of vertebrate DNA at the 5-position of ∼3–10% of its cytosine residues occurs in a sequence-specific and tissue-specific manner1–3 and has been implicated in the control of transcription1,4–7. How these differences are established and how they mediate the initiation or maintenance of transcription are unknown. DNA methylation might also have other roles, such as modulating DNA replication, transposition, DNA repair or chromosome configuration1,8,9. These other roles suggested for DNA methylation would be consistent with the finding that tissue-specific differences in methylation of certain gene regions5, highly repeated satellite DNA sequences8–10 and whole genomes2,3 often do not correlate with transcriptional activity. For DNA methylation to modulate the expression, maintenance or duplication of chromosomes, there should be effector macromolecules, presumably proteins, which specifically recognize 5-methylcytosine (m5C) residues in DNA. We describe here the first identification of a mammalian protein that binds preferentially to m5C-rich DNA sequences.
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Huang, LH., Wang, R., Gama-Sosa, M. et al. A protein from human placental nuclei binds preferentially to 5-methylcytosine-rich DNA. Nature 308, 293–295 (1984). https://doi.org/10.1038/308293a0
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DOI: https://doi.org/10.1038/308293a0
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