Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism

Kyohei Arita, Mariko Ariyoshi (), Hidehito Tochio, Yusuke Nakamura and Masahiro Shirakawa ()
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Kyohei Arita: Graduate School of Engineering, Kyoto University
Mariko Ariyoshi: Graduate School of Engineering, Kyoto University
Hidehito Tochio: Graduate School of Engineering, Kyoto University
Yusuke Nakamura: Laboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
Masahiro Shirakawa: Graduate School of Engineering, Kyoto University

Nature, 2008, vol. 455, issue 7214, 818-821

Abstract: Keeping DNA methylation on track DNA methylation is a key epigenetic process and the faithful maintenance of DNA methylation patterns is essential to the wellbeing of mammalian cells. This means that cells need a mechanism to identify the partially methylated version of CpG once a new DNA strand has been replicated or repaired, so that it can be further methylated by the DNA methyltransferase, DNMT1. As part of this process the protein UHRF1 (or Np95/ICBP90) facilitates the loading of DNMT1 onto the hemimethylated CpG sequences during DNA replication. Three papers in this issue describe crystal structures of the SRA domain of UHRF1 bound to DNA containing a hemi-methylated CpG site. The structures show that methyl-cytosine is flipped out of the DNA helix and inserted into a binding pocket on the SRA domain.

Date: 2008
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DOI: 10.1038/nature07249

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