De novo recruitment of Polycomb-group proteins in Drosophila embryos.

Autor:	Alhaj Abed J; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA., Ghotbi E; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA., Ye P; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA., Frolov A; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA., Benes J; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA., Jones RS; Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA rjones@smu.edu.
Jazyk:	angličtina
Zdroj:	Development (Cambridge, England) [Development] 2018 Nov 27; Vol. 145 (23). Date of Electronic Publication: 2018 Nov 27.
DOI:	10.1242/dev.165027
Abstrakt:	Polycomb-group (PcG)-mediated transcriptional repression of target genes can be delineated into two phases. First, following initial repression of target genes by gene-specific transcription factors, PcG proteins recognize the repressed state and assume control of the genes' repression. Second, once the silenced state is established, PcG proteins may maintain repression through an indefinite number of cell cycles. Little is understood about how PcG proteins initially recognize the repressed state of target genes and the steps leading to de novo establishment of PcG-mediated repression. We describe a genetic system in which a Drosophila PcG target gene, giant ( gt ), is ubiquitously repressed during early embryogenesis by a maternally expressed transcription factor, and show the temporal recruitment of components of three PcG protein complexes: PhoRC, PRC1 and PRC2. We show that de novo PcG recruitment follows a temporal hierarchy in which PhoRC stably localizes at the target gene at least 1 h before stable recruitment of PRC2 and concurrent trimethylation of histone H3 at lysine 27 (H3K27me3). The presence of PRC2 and increased levels of H3K27me3 are found to precede stable binding by PRC1. Competing Interests: Competing interestsThe authors declare no competing or financial interests. (© 2018. Published by The Company of Biologists Ltd.)
Databáze:	MEDLINE
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