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Enhanced top-down characterization of histone post-translational modifications.doc

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Enhanced top-down characterization of histone post-translational modifications

Tianetal.GenomeBiology2012,13:R86 /2012/13/10/R86 METHOD Open Access Enhancedtop-downcharacterizationofhistone post-translationalmodifications ZhixinTian1,2,NikolaToli?1,RuiZhao1,RonaldJMoore3,ShawnaMHengel1,ErrolWRobinson1,DavidLStenoien3, SiWu1,RichardDSmith3andLjiljanaPa?a-Toli?1* Abstract Post-translationalmodifications(PTMs)ofcorehistonesworksynergisticallytofinetunechromatinstructureand function,generatingaso-calledhistonecodethatcanbeinterpretedbyavarietyofchromatininteracting proteins.Wereportanovelonlinetwo-dimensionalliquidchromatography-tandemmassspectrometry(2DLC-MS/ MS)platformforhigh-throughputandsensitivecharacterizationofhistonePTMsattheintactproteinlevel.The platformenablesunambiguousidentificationof708histoneisoformsfromasingle2DLC-MS/MSanalysisof7.5μg purifiedcorehistones.Thethroughputandsensitivityofcomprehensivehistonemodificationcharacterizationis dramaticallyimprovedcomparedwithmoretraditionalplatforms. Keywords:SaltlessWCX-HILIC,top-down,histone,posttranslationalmodification Background PTMsdispersed alongtheentireprotein sequence that Histones are important chromatin proteins that actas havebeenpreviouslydiscoveredtohavesignificantparti- spools to package and order DNA into structural and cipationinchromatinregulation[2,9-11]. manageablechromosomes.Corehistonesaremodifiedby Top-downproteomicandhigh-throughputapproaches multiplepost-translationalmodifications(PTMs)suchas areclearlyrequiredtoidentifyandquantifythemodula- lysineacetylation,lysineorargininemethylation,andser- tion ofmultiple intra-molecular histone modifications ineorthreonine phosphorylation, amongothers.These thatsynergisticallyregulatehistonefunctions.Recently,a PTMsgeneratea‘histonecode’[1]thatisimplicated in global top-down study demonstrated the feasibility of chromatin-related cellular processes [2]includingtran- intact