YTH Domain: A Family of N 6 -methyladenosine (m 6 A) Readers

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Corrigendum: Structural basis for selective binding of m(6)A RNA by the YTHDC1 YTH domain.

Nat. Chem. Biol. 10, 927–929 (2014); published online 21 September 2014; corrected after print 19 August 2015 In the version of this Brief Communication initially published, the email address for corresponding author, Chao Xu, was incorrect. It should be listed as [email protected]. This error has been corrected in the PDF and HTML versions of the article. CORRIGENDUM Structural basis of en...

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Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain.

N(6)-methyladenosine (m(6)A) is the most abundant internal modification of nearly all eukaryotic mRNAs and has recently been reported to be recognized by the YTH domain family proteins. Here we present the crystal structures of the YTH domain of YTHDC1, a member of the YTH domain family, and its complex with an m(6)A-containing RNA. Our structural studies, together with transcriptome-wide ident...

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N 6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein

N6-methyladenosine (m6A) is the most abundant internal modification in eukaryotic messenger RNA (mRNA), and affects almost every stage of the mRNA life cycle. The YTH-domain proteins can specifically recognize m6A modification to control mRNA maturation, translation and decay. m6A can also alter RNA structures to affect RNA-protein interactions in cells. Here, we show that m6A increases the acc...

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Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA

N(6)A methylation is the most abundant RNA modification occurring within messenger RNA. Impairment of methylase or demethylase functions are associated with severe phenotypes and diseases in several organisms. Beside writer and eraser enzymes of this dynamic RNA epigenetic modification, reader proteins that recognize this modification are involved in numerous cellular processes. Although the pr...

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ژورنال

عنوان ژورنال: Genomics, Proteomics & Bioinformatics

سال: 2018

ISSN: 1672-0229

DOI: 10.1016/j.gpb.2018.04.002