Linker Histone H1.2 Cooperates with Cul4A and PAF1 to Drive H4K31 Ubiquitylation-Mediated Transactivation

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Increasing evidence suggests that linker histone H1 can influence distinct cellular processes by acting as a gene-specific regulator. However, the mechanistic basis underlying such H1 specificity and whether H1 acts in concert with other chromatin-altering activities remain unclear. Here, we show that one of the H1 subtypes, H1.2, stably interacts with Cul4A E3 ubiquitin ligase and PAF1 elongation complexes and that such interaction potentiates target gene transcription via induction of H4K31ubiquitylation, H3K4me3, and H3K79me2. H1.2, Cul4A, and PAF1 are functionally cooperative because their individual knockdown results in the loss of the corresponding histone marks and the deficiency of target gene transcription. H1.2 interacts with the serine 2-phosphorylated form of RNAPII, and we argue that it recruits the Cul4A and PAF1 complexes to target genes by bridging the interaction between the Cul4A and PAF1 complexes. These data define an expanded role for H1 in regulating gene transcription and illustrate its dependence on the elongation competence of RNAPII.
Publisher
Cell Press
Issue Date
2013-12
Language
English
Article Type
Article
Keywords

DNA-DAMAGE RESPONSE; GENE-EXPRESSION; H3K4 METHYLATION; TRANSCRIPTIONAL ELONGATION; CAENORHABDITIS-ELEGANS; WD40-REPEAT PROTEINS; H2B UBIQUITYLATION; POLYMERASE-II; IN-VIVO; COMPLEX

Citation

CELL REPORTS, v.5, no.6, pp.1690 - 1703

ISSN
2211-1247
DOI
10.1016/j.celrep.2013.11.038
URI
http://hdl.handle.net/10203/201293
Appears in Collection
BS-Journal Papers(저널논문)
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