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

Hideharu Hashimoto, June E. Pais, Xing Zhang, Lana Saleh, Zheng-Qing Fu, Nan Dai, Ivan R. Corrêa, Yu Zheng () and Xiaodong Cheng ()
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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
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

Nature, 2014, vol. 506, issue 7488, 391-395

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.

Date: 2014
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DOI: 10.1038/nature12905

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