2014
Histone Variant H2A.X Deposition Pattern Serves as a Functional Epigenetic Mark for Distinguishing the Developmental Potentials of iPSCs
Wu T, Liu Y, Wen D, Tseng Z, Tahmasian M, Zhong M, Rafii S, Stadtfeld M, Hochedlinger K, Xiao A. Histone Variant H2A.X Deposition Pattern Serves as a Functional Epigenetic Mark for Distinguishing the Developmental Potentials of iPSCs. Cell Stem Cell 2014, 15: 281-294. PMID: 25192463, DOI: 10.1016/j.stem.2014.06.004.Peer-Reviewed Original ResearchConceptsEmbryonic stem cellsLineage gene expressionHistone variant H2A.XCell lineage commitmentDevelopmental potentialMouse iPSC linesIPSC linesPluripotent stem cell (iPSC) technologyEpigenetic marksLineage genesEpigenetic mechanismsLineage commitmentLineage differentiationExtraembryonic differentiationStem cell technologyGene expressionTetraploid complementationIPSC clonesIPSC qualityStem cellsFunctional markersH2A.XDifferentiationIPSCsComplementationUsing Native Chromatin Immunoprecipitation to Interrogate Histone Variant Protein Deposition in Embryonic Stem Cells
Tseng Z, Wu T, Liu Y, Zhong M, Xiao A. Using Native Chromatin Immunoprecipitation to Interrogate Histone Variant Protein Deposition in Embryonic Stem Cells. Methods In Molecular Biology 2014, 1176: 11-22. PMID: 25030915, DOI: 10.1007/978-1-4939-0992-6_2.Peer-Reviewed Original ResearchConceptsNative chromatin immunoprecipitationHigh-throughput sequencingEmbryonic stem cellsChromatin immunoprecipitationHistone variantsMouse embryonic stem cellsGenome-wide localizationChromatin-associated factorsStem cellsProtein of interestMassive parallel sequencingHistone modificationsChromatin regionsChromatin pelletEpigenetic techniquesDNA fragmentsParallel sequencingImmunoprecipitationLibrary constructionSequencingEnzymatic digestionProtein depositionCellsH2A.XSpecific antibodies
2009
Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*
Krishnan N, Jeong DG, Jung SK, Ryu SE, Xiao A, Allis CD, Kim SJ, Tonks NK. Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*. Journal Of Biological Chemistry 2009, 284: 16066-16070. PMID: 19351884, PMCID: PMC2713548, DOI: 10.1074/jbc.c900032200.Peer-Reviewed Original ResearchMeSH KeywordsCell Line, TumorDNA DamageDNA-Binding ProteinsElectrochemistryHistonesHumansIntracellular Signaling Peptides and ProteinsMetalsNuclear ProteinsPhosphorylationProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesRNA InterferenceSubstrate SpecificityTransfectionTyrosineConceptsEyes AbsentDNA damage responseTyr-142Damage responseTyrosyl residuesProtein tyrosine phosphataseDNA damage repairAtypical kinaseHistone H2A.X.Haloacid dehalogenaseMammalian cellsHistone H2A.XDisplayed specificityElevated basal phosphorylationPhosphorylation statusRNA interferenceDamage repairPhysiological substratesH2A.XNovel roleBasal phosphorylationImportant regulatorDephosphorylationResiduesWSTFA distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint
Shechter D, Chitta RK, Xiao A, Shabanowitz J, Hunt DF, Allis CD. A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 749-754. PMID: 19131518, PMCID: PMC2630098, DOI: 10.1073/pnas.0812207106.Peer-Reviewed Original ResearchConceptsDNA damageEarly embryosSignificance of phosphorylationTerminal consensus sequenceExogenous DNA damageDNA damage responseCell-free egg extractsPhospho-specific antibodiesEarly cell cyclesFrog Xenopus laevisMulticellular organismsH2A variantsXenopus tropicalisDamage responseUnannotated isoformsMammalian cellsHistone H2A.XSomatic cellsCheckpoint conditionsXenopus laevis eggsAquatic speciesEgg extractsConsensus sequenceCell cycleH2A.X