Abstract:
:Trimethylation of histone H3 on lysine 4 (H3K4me3) localizes near the 5' region of genes and is tightly associated with active loci. Several proteins, such as CHD1, BPTF, JMJD2A, and the ING tumor suppressor family, directly recognize this lysine methyl mark. However, how H3K4me3 recognition participates in active transcription remains poorly characterized. Here we identify specific CHD1-interacting proteins via H3K4me3 affinity purification, including numerous factors mediating postinitiation events. Conventional biochemical purification revealed a stable complex between CHD1 and components of the spliceosome. Depletion of CHD1 in extracts dramatically reduced splicing efficiency in vitro, indicating a functional link between CHD1 and the spliceosome. Knockdown of CHD1 and H3K4me3 levels by siRNA reduced association of U2 snRNP components with chromatin and, more importantly, altered the efficiency of pre-mRNA splicing on active genes in vivo. These findings suggest that methylated H3K4 serves to facilitate the competency of pre-mRNA maturation through the bridging of spliceosomal components to H3K4me3 via CHD1.
journal_name
Mol Celljournal_title
Molecular cellauthors
Sims RJ 3rd,Millhouse S,Chen CF,Lewis BA,Erdjument-Bromage H,Tempst P,Manley JL,Reinberg Ddoi
10.1016/j.molcel.2007.11.010subject
Has Abstractpub_date
2007-11-30 00:00:00pages
665-76issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(07)00744-7journal_volume
28pub_type
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