The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix

Hideharu Hashimoto, John R. Horton, Xing Zhang, Magnolia Bostick, Steven E. Jacobsen and Xiaodong Cheng ()
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Hideharu Hashimoto: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
John R. Horton: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Xing Zhang: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA
Magnolia Bostick: Department of Molecular Cell and Developmental Biology,
Steven E. Jacobsen: Department of Molecular Cell and Developmental Biology,
Xiaodong Cheng: Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA

Nature, 2008, vol. 455, issue 7214, 826-829

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/nature07280

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