2022
The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication
Davarinejad H, Huang YC, Mermaz B, LeBlanc C, Poulet A, Thomson G, Joly V, Muñoz M, Arvanitis-Vigneault A, Valsakumar D, Villarino G, Ross A, Rotstein BH, Alarcon EI, Brunzelle JS, Voigt P, Dong J, Couture JF, Jacob Y. The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication. Science 2022, 375: 1281-1286. PMID: 35298257, PMCID: PMC9153895, DOI: 10.1126/science.abm5320.Peer-Reviewed Original ResearchConceptsTetratricopeptide repeat domainDNA polymerase thetaMulticellular eukaryotesHistone H3.1Replication forksChromatin maturationRepeat domainDNA repairGenomic instabilityPolymerase thetaPosition 31Amino acidsH3.1PlantsReplicationEukaryotesH3.3HistonesMonomethylationVariantsCommon strategyForkResiduesMaturationFunction
2021
H3.1K27me1 maintains transcriptional silencing and genome stability by preventing GCN5-mediated histone acetylation
Dong J, LeBlanc C, Poulet A, Mermaz B, Villarino G, Webb KM, Joly V, Mendez J, Voigt P, Jacob Y. H3.1K27me1 maintains transcriptional silencing and genome stability by preventing GCN5-mediated histone acetylation. The Plant Cell 2021, 33: 961-979. PMID: 33793815, PMCID: PMC8226292, DOI: 10.1093/plcell/koaa027.Peer-Reviewed Original ResearchConceptsGenome stabilityGenomic instabilityHistone acetylationSAGA-like complexesMultiple lysine residuesArabidopsis GCN5ARABIDOPSIS TRITHORAXArabidopsis thalianaTranscriptional silencingHeterochromatin defectsDouble mutantDNA replicationEpigenetic mechanismsGCN5Molecular roleEssential functionsDiverse rolesMolecular mechanismsLysine residuesProtein 5AcetylationMutantsPlantsADA2bATXR6
2010
Regulation of heterochromatic DNA replication by histone H3 lysine 27 methyltransferases
Jacob Y, Stroud H, LeBlanc C, Feng S, Zhuo L, Caro E, Hassel C, Gutierrez C, Michaels SD, Jacobsen SE. Regulation of heterochromatic DNA replication by histone H3 lysine 27 methyltransferases. Nature 2010, 466: 987-991. PMID: 20631708, PMCID: PMC2964344, DOI: 10.1038/nature09290.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsArabidopsisArabidopsis ProteinsCatalytic DomainDNA MethylationDNA ReplicationDNA Transposable ElementsDNA, PlantGene Expression Regulation, PlantGene SilencingGenome, PlantHeterochromatinHistone-Lysine N-MethyltransferaseHistonesLysineMethylationMethyltransferasesMutant ProteinsMutationReplication Origin
2009
ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing
Jacob Y, Feng S, LeBlanc CA, Bernatavichute YV, Stroud H, Cokus S, Johnson LM, Pellegrini M, Jacobsen SE, Michaels SD. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nature Structural & Molecular Biology 2009, 16: 763-768. PMID: 19503079, PMCID: PMC2754316, DOI: 10.1038/nsmb.1611.Peer-Reviewed Original Research