Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain

• Published in: PloS one Vol. 6; no. 6; p. e21306
• Main Authors: Frauer, Carina, Hoffmann, Thomas, Bultmann, Sebastian, Casa, Valentina, Cardoso, M Cristina, Antes, Iris, Leonhardt, Heinrich
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 22.06.2011; Public Library of Science (PLoS)
• Subjects: 5-Methylcytosine - metabolism; Algorithms; Binding Sites; Biology; CCAAT-Enhancer-Binding Proteins - chemistry; CCAAT-Enhancer-Binding Proteins - metabolism; Cellular proteins; Competition; Computer Science; CpG islands; CpG Islands - genetics; Crystal structure; Cytosine; Cytosine - analogs & derivatives; Cytosine - metabolism; Deoxyribonucleic acid; DNA; DNA - chemistry; DNA - metabolism; DNA methylation; Epigenetic inheritance; Epigenetics; Gene expression; HEK293 Cells; Humans; Hydrogen; Hydrogen Bonding; Hydrogen bonds; Hydroxides; Hydroxyl groups; Life sciences; Mammals; MeCP2 protein; Methyl-CpG binding protein; Methylation; Molecular dynamics; Molecular Dynamics Simulation; Molecular structure; Physical chemistry; Physics; Protein Binding; Protein Structure, Tertiary; Proteins; Pyrimidines; Stem cells; Studies; Substrates; Thermodynamics; Germany

Recent discovery of 5-hydroxymethylcytosine (5hmC) in genomic DNA raises the question how this sixth base is recognized by cellular proteins. In contrast to the methyl-CpG binding domain (MBD) of MeCP2, we found that the SRA domain of Uhrf1, an essential factor in DNA maintenance methylation, binds...