| Literature DB >> 34324427 |
Abdulkhaleg Ibrahim1,2,3,4,5,6, Christophe Papin1,2,3,4,5, Kareem Mohideen-Abdul1,3,4,5,7, Stéphanie Le Gras1,3,4,5, Isabelle Stoll1,2,3,4,5, Christian Bronner1,2,3,4,5, Stefan Dimitrov8,9, Bruno P Klaholz10,3,4,5,7, Ali Hamiche10,2,3,4,5,7,11.
Abstract
The Rett syndrome protein MeCP2 was described as a methyl-CpG-binding protein, but its exact function remains unknown. Here we show that mouse MeCP2 is a microsatellite binding protein that specifically recognizes hydroxymethylated CA repeats. Depletion of MeCP2 alters chromatin organization of CA repeats and lamina-associated domains and results in nucleosome accumulation on CA repeats and genome-wide transcriptional dysregulation. The structure of MeCP2 in complex with a hydroxymethylated CA repeat reveals a characteristic DNA shape, with considerably modified geometry at the 5-hydroxymethylcytosine, which is recognized specifically by Arg133, a key residue whose mutation causes Rett syndrome. Our work identifies MeCP2 as a microsatellite DNA binding protein that targets the 5hmC-modified CA-rich strand and maintains genome regions nucleosome-free, suggesting a role for MeCP2 dysfunction in Rett syndrome.Entities:
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Year: 2021 PMID: 34324427 DOI: 10.1126/science.abd5581
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728