Structural peculiarities of the (MHF1-MHF2)4 octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: a solution SAXS study.

Wenjia Wang, Qiong Guo, Eleonora V Shtykova, Guangfeng Liu, Jianhua Xu, Maikun Teng, Peng Liu, Yuhui Dong

FEBS letters 2013 Sep 17

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MHF1 and MHF2 are histone-fold-containing FANCM-associated proteins. FANCM is a Fanconi anemia (FA) complementation group protein. We previously obtained high-resolution structures of MHF1-MHF2 (MHF) and MHF in complex with a fragment of FANCM (MHF-FANCM-F). Here, we use small angle X-ray scattering (SAXS) to investigate the solution behaviors of these protein complexes. In combination with crystallographic data, the results of the SAXS study reveal that a long, positively charged patch exposed on the surface of the MHF complex plays a critical role in double-stranded DNA (dsDNA) binding. Copyright © 2013. Published by Elsevier B.V.

Citation

Wenjia Wang, Qiong Guo, Eleonora V Shtykova, Guangfeng Liu, Jianhua Xu, Maikun Teng, Peng Liu, Yuhui Dong. Structural peculiarities of the (MHF1-MHF2)4 octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: a solution SAXS study. FEBS letters. 2013 Sep 17;587(18):2912-7