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Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription
Author(s) -
Ardehali M Behfar,
Mei Amanda,
Zobeck Katie L,
Caron Matthieu,
Lis John T,
Kusch Thomas
Publication year - 2011
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2011.194
Subject(s) - biology , histone , histone h3 , transcription (linguistics) , genetics , lysine , histone code , drosophila melanogaster , microbiology and biotechnology , transcription factor , histone methyltransferase , nucleosome , dna , gene , amino acid , linguistics , philosophy
Histone H3 lysine 4 trimethylation (H3K4me3) is a major hallmark of promoter‐proximal histones at transcribed genes. Here, we report that a previously uncharacterized Drosophila H3K4 methyltransferase, dSet1, and not the other putative histone H3K4 methyltransferases (Trithorax; Trithorax‐related protein), is predominantly responsible for histone H3K4 trimethylation. Functional and proteomics studies reveal that dSet1 is a component of a conserved H3K4 trimethyltransferase complex and polytene staining and live cell imaging assays show widespread association of dSet1 with transcriptionally active genes. dSet1 is present at the promoter region of all tested genes, including activated Hsp70 and Hsp26 heat shock genes and is required for optimal mRNA accumulation from the tested genes. In the case of Hsp70 , the mRNA production defect in dSet1 RNAi‐treated cells is accompanied by retention of Pol II at promoters. Our data suggest that dSet1‐dependent H3K4me3 is responsible for the generation of a chromatin structure at active promoters that ensures optimal Pol II release into productive elongation.