Cell Cycle– and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast 英文参考文献.docVIP

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Cell Cycle– and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast 英文参考文献.doc

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Cell Cycle– and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast 英文参考文献

CellCycle–andChaperone-MediatedRegulationof H3K56acIncorporationinYeast TommyKaplan1,2.,ChihLongLiu3.¤,JudithA.Erkmann4.,JohnHolik3,MichaelGrunstein5,6,PaulD. Kaufman4*,NirFriedman1*,OliverJ.Rando3* 1SchoolofComputerScienceandEngineering,TheHebrewUniversity,Jerusalem,Israel,2DepartmentofMolecularGeneticsandBiotechnology,FacultyofMedicine, The Hebrew University, Jerusalem, Israel, 3Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts,UnitedStatesofAmerica,4ProgramsinGeneFunctionandExpressionandMolecularMedicine,UniversityofMassachusettsMedicalSchool,Worcester, Massachusetts,UnitedStatesofAmerica,5DepartmentofBiologicalChemistry,GeffenSchoolofMedicine,UniversityofCaliforniaLosAngeles,LosAngeles,California, UnitedStatesofAmerica,6MolecularBiologyInstitute,LosAngeles,California,UnitedStatesofAmerica Abstract AcetylationofhistoneH3lysine56isacovalentmodificationbestknownasamarkofnewlyreplicatedchromatin,butithas alsobeenlinkedtoreplication-independenthistonereplacement.Here,wemeasuredH3K56aclevelsatsingle-nucleosome resolutioninasynchronouslygrowingyeastcultures,aswellasinyeastproceedingsynchronouslythroughthecellcycle. WedevelopedaquantitativemodelofH3K56ackinetics,whichshowsthatH3K56acislargelyexplainedbythegenomic replicationtimingandtheturnoverrateofeachnucleosome,suggestingthatcellcycleprofilesofH3K56acshouldreveal most first-time nucleosome incorporation events. However, since the deacetylases Hst3/4 prevent use of H3K56ac as a markerforhistonedepositionduringMphase,wealsodirectlymeasuredMphasehistonereplacementrates.Wereporta global decrease in turnover rates during M phase and a further specific decrease in turnover at several early origins of replication, which switch from rapidly replaced in G1 phase to stably bound during M phase. Finally, by measuring H3 replacementinyeastdeletedfortheH3K56acetyltransferaseRtt109anditstwoco-chaperonesAsf1andVps75,wefind evidencethatRtt109andAsf1preferent