Systematic analysis of the binding behaviour of UHRF1 towards different methyl- and carboxylcytosine modification patterns at CpG dyads.

Systematic analysis of the binding behaviour of UHRF1 towards different methyl- and carboxylcytosine modification patterns at CpG dyads.

The multi-domain protein UHRF1 is essential for DNA methylation maintenance and binds DNA via a base-flipping mechanism with a preference for hemi-methylated CpG sites. We investigated its binding to hemi- and symmetrically modified DNA containing either 5-methylcytosine (mC), 5-hydroxymethylcytosin...

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Bibliographic Details
Main Authors: Markus Schneider, Carina Trummer, Andreas Stengl, Peng Zhang, Aleksandra Szwagierczak, M Cristina Cardoso, Heinrich Leonhardt, Christina Bauer, Iris Antes
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2020-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0229144

Internet

https://doi.org/10.1371/journal.pone.0229144

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