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The structure of the FANCM–MHF complex reveals physical features for functional assembly

Author

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  • Yuyong Tao

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences)

  • Changjiang Jin

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences
    Anhui-MSM Joint Research Group for Cellular Dynamics, Anhui Key Laboratory for Cellular Dynamics Chemical Biology)

  • Xu Li

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences)

  • Shali Qi

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences)

  • Lingluo Chu

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences
    Anhui-MSM Joint Research Group for Cellular Dynamics, Anhui Key Laboratory for Cellular Dynamics Chemical Biology)

  • Liwen Niu

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences)

  • Xuebiao Yao

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences
    Anhui-MSM Joint Research Group for Cellular Dynamics, Anhui Key Laboratory for Cellular Dynamics Chemical Biology)

  • Maikun Teng

    (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
    Key Laboratory of Structural Biology, Chinese Academy of Sciences)

Abstract

Fanconi anaemia is a rare genetic disease characterized by chromosomal instability and cancer susceptibility. The Fanconi anaemia complementation group protein M (FANCM) forms an evolutionarily conserved DNA-processing complex with MHF1/MHF2 (histone-fold-containing proteins), which is essential for DNA repair in response to genotoxic stress. Here we present the crystal structures of the MHF1–MHF2 complex alone and bound to a fragment of FANCM (FANCM661−800, designated FANCM-F). The structures show that MHF1 and MHF2 form a compact tetramer to which FANCM-F binds through a 'dual-V' shaped structure. FANCM-F and (MHF1–MHF2)2 cooperate to constitute a new DNA-binding site that is coupled to the canonical L1L2 region. Perturbation of the MHF–FANCM-F structural plasticity changes the localization of FANCM in vivo. The MHF–FANCM interaction and its subcellular localization are altered by a disease-associated mutant of FANCM. These findings reveal the molecular basis of MHF–FANCM recognition and provide mechanistic insights into the pathway leading to Fanconi anaemia.

Suggested Citation

  • Yuyong Tao & Changjiang Jin & Xu Li & Shali Qi & Lingluo Chu & Liwen Niu & Xuebiao Yao & Maikun Teng, 2012. "The structure of the FANCM–MHF complex reveals physical features for functional assembly," Nature Communications, Nature, vol. 3(1), pages 1-12, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1779
    DOI: 10.1038/ncomms1779
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