HistonechaperonenetworksshapingchromatinfunctionColinM.Hammond1,*,CarolineB.Strømme1,*,HongdaHuang2,DinshawJ.Patel2,andAnjaGroth11BiotechResearchandInnovationCentre(BRIC)andCentreforEpigenetics,FacultyofHealthandMedicalSciences,UniversityofCopenhagen,CopenhagenDK-2200,Denmark2StructuralBiologyProgram,MemorialSloan-KetteringCancerCenter,NewYork,NewYork10065,USAAbstractTheassociationofhistoneswithspecificchaperonecomplexesisimportantfortheirfolding,oligomerization,post-translationalmodification,nuclearimport,stability,assemblyandgenomiclocalization.Inthisway,thechaperoningofsolublehistonesisakeydeterminantofhistoneavailabilityandfate,whichaffectsallchromosomalprocesses,includinggeneexpression,chromosomesegregationandgenomereplicationandrepair.Here,wereviewthedistinctstructuralandfunctionalpropertiesoftheexpandingnetworkofhistonechaperones.Weemphasizehowchaperonescooperateinthehistonechaperonenetworkandviaco-chaperonecomplexestomatchhistonesupplywithdemand,therebypromotingpropernucleosomeassemblyandmaintainingepigeneticinformationbyrecyclingmodifiedhistonesevictedfromchromatin.ToCblurbHistonechaperonessafeguardthechromatintemplateandshieldhistonesfrompromiscuousinteractionstoensuretheirproperstorage,transport,post-translationalmodification,nucleosomeassemblyandturnover.Nucleosomes(BOX1),whichrestrictDNAaccessibility,mustbehighlydynamicintermsoftheirpositioningandstateofassemblytoallowaccesstothebaseread-outofDNA.ThemodularnatureofnucleosomesprovidesfunctionalcomplexitythroughtheincorporationofCorrespondencetoA.G.anja.groth@bric.ku.dk.*Theseauthorscontributedequallytothiswork.CompetinginterestsstatementTheauthorsdeclarecompetingfinancialinterests:C.M.H.,H.H.,D.J.P.andA.G.arenamedinventorsonapatentapplicationcoveringthediscoveriesinSaredietal.H4K20me0markspost-replicativechromatinandrecruitstheTONSL–MMS22LDNArepaircomplex.Nature534,714–718(2016).DATABASESRSCBProteinDataBank:http://www.rcsb.org/pdb/home/home.doSGDYeastMine:http://yeastmine.yeastgenome.orgALLLINKSARE...
