Nucleosome Disruption by DNA Ligase III-XRCC1 Promotes Efficient Base Excision Repair
Odell ID, Barbour JE, Murphy DL, Della-Maria JA, Sweasy JB, Tomkinson AE, Wallace SS, Pederson DS. Nucleosome Disruption by DNA Ligase III-XRCC1 Promotes Efficient Base Excision Repair. Molecular And Cellular Biology 2011, 31: 4623-4632. PMID: 21930793, PMCID: PMC3209256, DOI: 10.1128/mcb.05715-11.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDeoxyribonuclease (Pyrimidine Dimer)DNADNA DamageDNA GlycosylasesDNA Ligase ATPDNA LigasesDNA Polymerase betaDNA RepairDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsHumansLytechinusNucleosomesPoly-ADP-Ribose Binding ProteinsReactive Oxygen SpeciesX-ray Repair Cross Complementing Protein 1XenopusXenopus ProteinsConceptsBase excision repairNucleosome disruptionApurinic endonucleaseExcision repairEfficient base excision repairNucleated human cellsDNA polymerase βNucleosome substratesRibosomal DNASingle base gapHuman cellsNucleosomesDNA ligasePolymerase βPol βRate-limiting stepHNTH1Ternary complexDNAUnique roleChromatinLigaseDisruptionEndonucleaseLesions form