BioProject

How different histone methyltransferases (HMT) cooperate to progressively catalyze different methylation states of the same residue as well the functional consequences of the different methylation states are not well known. More...

How different histone methyltransferases (HMT) cooperate to progressively catalyze different methylation states of the same residue as well the functional consequences of the different methylation states are not well known. Here, we address in the context of Drosophila H3K36 methylation by using single and combinatorial RNAi of HMTs along with genome-wide MNase-ChIPseq analyses. Our study reveals that K36me1/2/3 each mark distinct chromatin compartments. Each HMT predominantly contributes to only one modification state, however our approach also identifies context-dependent cooperative and compensative patterns. Further, correlating changes in K36me1/2/3 to reader binding reveals that K36me2/3 can redundantly contribute to faithful reader binding ensuring robustness. Overall design: MNase Chromatin Immunoprecipitation DNA Sequencing (ChIP-seq) for K36me1/2/3, K27me3, K9me2, HMTs(ePol, Mes4) and readers (JASPer/PW, Msl3) in RNAi treated (10/7 days; RNAi targets - GST/GFP=Control, Set2, NSD,Ash1, Comb=Set2+NSD) S2 cells Less...