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TY - JOUR AU - Arita, Kyohei AU - Ariyoshi, Mariko AU - Tochio, Hidehito AU - Nakamura, Yusuke AU - Shirakawa, Masahiro PY - 2008 DA - 2008/10/01 TI - Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism JO - Nature SP - 818 EP - 821 VL - 455 IS - 7214 AB - 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. SN - 1476-4687 UR - https://doi.org/10.1038/nature07249 DO - 10.1038/nature07249 ID - Arita2008 ER -