Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1

George V. Avvakumov, John R. Walker, Sheng Xue, Yanjun Li, Shili Duan, Christian Bronner, Cheryl H. Arrowsmith and Sirano Dhe-Paganon ()
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George V. Avvakumov: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
John R. Walker: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
Sheng Xue: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
Yanjun Li: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
Shili Duan: University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada
Christian Bronner: CNRS UMR 7175, IGL, Université Louis Pasteur Strasbourg I, Faculté de Pharmacie, 74 route du Rhin, B.P. 60024, 67401 Illkirch, France
Cheryl H. Arrowsmith: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
Sirano Dhe-Paganon: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada

Nature, 2008, vol. 455, issue 7214, 822-825

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/nature07273

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