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Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA

Author

Listed:
  • Hideharu Hashimoto

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

  • June E. Pais

    (New England Biolabs, 240 County Road)

  • Xing Zhang

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

  • Lana Saleh

    (New England Biolabs, 240 County Road)

  • Zheng-Qing Fu

    (University of Georgia
    Sector 22, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439, USA)

  • Nan Dai

    (New England Biolabs, 240 County Road)

  • Ivan R. Corrêa

    (New England Biolabs, 240 County Road)

  • Yu Zheng

    (New England Biolabs, 240 County Road)

  • Xiaodong Cheng

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

Abstract

The Tet family of dioxygenase enzymes convert 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine and 5-carboxylcytosine, which has an effect on gene expression; here the structure of NgTet1, a Tet-like protein with the same activity as mammalian Tet1, is determined, showing that NgTet1 uses a base-flipping mechanism to access 5-methylcytosine.

Suggested Citation

  • Hideharu Hashimoto & June E. Pais & Xing Zhang & Lana Saleh & Zheng-Qing Fu & Nan Dai & Ivan R. Corrêa & Yu Zheng & Xiaodong Cheng, 2014. "Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA," Nature, Nature, vol. 506(7488), pages 391-395, February.
    • Handle: RePEc:nat:nature:v:506:y:2014:i:7488:d:10.1038_nature12905
    DOI: 10.1038/nature12905
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