Structural highlights
FunctionYTDC1_RAT RNA-binding protein that regulates alternative splice site selection.[1] [2] Publication Abstract from PubMedN6A 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 precise characterization of these reader proteins remains unknown, preliminary data showed that most potential reader proteins contained a conserved YT521-B homology (YTH) domain. Here we define the YTH domain of rat YT521-B as a N6-methylated adenosine reader domain and report its solution structure in complex with a N6-methylated RNA. The structure reveals a binding preference for NGANNN RNA hexamer and a deep hydrophobic cleft for m6A recognition. These findings establish a molecular function for YTH domains as m6A reader domains and should guide further studies into the biological functions of YTH-containing proteins in m6A recognition. Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA.,Theler D, Dominguez C, Blatter M, Boudet J, Allain FH Nucleic Acids Res. 2014 Nov 11. pii: gku1116. PMID:25389274[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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