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

摘要

MHF1andMHF2arehistone‐fold‐containingFANCM‐associatedproteins.FANCMisaFanconianemia(FA)complementationgroupprotein.Wepreviouslyobtainedhigh‐resolutionstructuresofMHF1–MHF2(MHF)andMHFincomplexwithafragmentofFANCM(MHF–FANCM‐F).Here,weusesmallangleX‐rayscattering(SAXS)toinvestigatethesolutionbehaviorsoftheseproteincomplexes.Incombinationwithcrystallographicdata,theresultsoftheSAXSstudyrevealthatalong,positivelychargedpatchexposedonthesurfaceoftheMHFcomplexplaysacriticalroleindouble‐strandedDNA(dsDNA)binding...