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

Yuyong Tao, Changjiang Jin, Xu Li, Shali Qi, Lingluo Chu, Liwen Niu, Xuebiao Yao () and Maikun Teng ()
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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
Changjiang Jin: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Xu Li: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Shali Qi: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Lingluo Chu: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Liwen Niu: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Xuebiao Yao: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China
Maikun Teng: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China

Nature Communications, 2012, vol. 3, issue 1, 1-12

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms1779

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