Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 33, Issue 24, Pages 4936-4946Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.00601-13
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Funding
- March of Dimes grant
- National Institutes of Health [DK064678, NS054941, DK071900, CA148354]
- Basic Science Research Program [2012R1A1A1001749]
- Bio and Medical Technology Development Program [2012M3A9C6050508]
- National Research Foundation funded by the Republic of South Korea (MEST)
- National R& D Program for Cancer Control, Ministry of Health and Welfare, Republic of Korea [1220120]
- Ministry of Education, Science and Technology [R3110105]
- National Research Foundation of Korea
- Korea Health Promotion Institute [1220120] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Trimethylated histone H3 lysine 4 (H3K4) and H3K27 generally mark transcriptionally active and repressive chromatins, respectively. In most cell types, these two modifications are mutually exclusive, and this segregation is crucial for the regulation of gene expression. However, how this anticorrelation is achieved has not been fully understood. Here, we show that removal of the H3K27 trimethyl mark facilitates recruitment of SET1-like H3K4 methyltransferase complexes to their target genes by eliciting a novel interaction between histone H3 and two common subunits, WDR5 and RBBP5, of SET1-like complexes. Consistent with this result, H3K27 trimethylation destabilizes interactions of H3 with SET1-like complexes and antagonizes their ability to carry out H3K4 trimethylation of peptide (H3 residues 1 to 36), histone octamer, and mononucleosome substrates. Altogether, our studies reveal that H3K27 trimethylation of histone H3 represses a previously unrecognized interaction between H3 and SET1like complexes. This provides an important mechanism that directs the anticorrelation between H3K4 and H3K27 trimethylation.
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