Biochemical and structural basis for YTH domain of human YTHDC1 binding to methylated adenine in DNA

The recently characterized mammalian writer (methyltransferase) and eraser (demethylase) of the DNA N6-methyladenine (N6mA) methyl mark act on single-stranded (ss) and transiently-unpaired DNA. As YTH domain-containing proteins bind N6mA-containing RNA in mammalian cells, we investigated whether mam...

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Veröffentlicht in:	Nucleic acids research 2020-10, Vol.48 (18), p.10329-10341
Hauptverfasser:	Woodcock, Clayton B, Horton, John R, Zhou, Jujun, Bedford, Mark T, Blumenthal, Robert M, Zhang, Xing, Cheng, Xiaodong
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenine - chemistry BASIC BIOLOGICAL SCIENCES DNA - chemistry DNA - genetics DNA - ultrastructure DNA, Single-Stranded - chemistry DNA, Single-Stranded - genetics Genome integrity Genome Integrity, Repair and Histone Demethylases - genetics Humans INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY Methylation Methyltransferases - genetics Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - ultrastructure Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - ultrastructure Protein Conformation Protein Domains - genetics repair and replication RNA Splicing Factors - chemistry RNA Splicing Factors - genetics RNA Splicing Factors - ultrastructure RNA-Binding Proteins - genetics
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