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

Author

Listed:
  • 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
    University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada)

  • Sirano Dhe-Paganon

    (Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada
    University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada)

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.

Suggested Citation

  • George V. Avvakumov & John R. Walker & Sheng Xue & Yanjun Li & Shili Duan & Christian Bronner & Cheryl H. Arrowsmith & Sirano Dhe-Paganon, 2008. "Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1," Nature, Nature, vol. 455(7214), pages 822-825, October.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7214:d:10.1038_nature07273
    DOI: 10.1038/nature07273
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    Cited by:

    1. Amika Kikuchi & Hiroki Onoda & Kosuke Yamaguchi & Satomi Kori & Shun Matsuzawa & Yoshie Chiba & Shota Tanimoto & Sae Yoshimi & Hiroki Sato & Atsushi Yamagata & Mikako Shirouzu & Naruhiko Adachi & Jafa, 2022. "Structural basis for activation of DNMT1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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