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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
Author(s) -
Wang Wenjia,
Guo Qiong,
Shtykova Eleonora V.,
Liu Guangfeng,
Xu Jianhua,
Teng Maikun,
Liu Peng,
Dong Yuhui
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.022
Subject(s) - small angle x ray scattering , histone octamer , fanconi anemia , dna , crystallography , chromatin , nucleosome , biology , chemistry , biophysics , biochemistry , scattering , dna repair , physics , optics
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.