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Abstract
Modifications to the core histones are thought to contribute to ESC pluripotency by
priming tissue-specific promoters and enhancers for later activation. However, it
is unclear how these marks are targeted in ESCs and maintained during differentiation.
Here, we show that the ESC factor Sox2 targets H3K4 methylation to monovalent and
bivalent domains. In ESCs, Sox2 contributes to the formation of a monovalent mark
at an enhancer in the pro/pre-B cell-specific lambda5-VpreB1 locus. Binding of Foxd3
suppresses intergenic transcription of the enhancer and surrounding sequences. In
pro-B cells, enhancer activity is dependent on the Sox and Fox binding sites, and
the enhancer is bound by Sox4, which is required for efficient expression of lambda5.
Our results lead us to propose a factor relay model whereby ESC factors establish
active epigenetic marks at tissue specific elements before being replaced by cell
type-specific factors as cells differentiate.
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