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ALFIN-LIKE proteins bind H3K4me3 and recruit SWR1 to repress responsive genes [ChIP-Seq]

ABSTRACT: ALFIN-LIKE proteins bind H3K4me3 and recruit SWR1 to repress responsive genes [ChIP-Seq]

PROVIDER: PRJNA1128659 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29564200_1.fastq.gz	Fastqsanger.gz
	SRR29564200_2.fastq.gz	Fastqsanger.gz
	SRR29564201_1.fastq.gz	Fastqsanger.gz
	SRR29564201_2.fastq.gz	Fastqsanger.gz
	SRR29564202_1.fastq.gz	Fastqsanger.gz

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ALFIN-LIKE proteins bind H3K4me3 and recruit SWR1 to repress responsive genes [RNA-Seq]

Project description:ALFIN-LIKE proteins bind H3K4me3 and recruit SWR1 to repress responsive genes [RNA-Seq]

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ALFIN-LIKE proteins bind H3K4me3 and recruit SWR1 to repress responsive genes [RNA-Seq]

Project description:In eukaryotes, the canonical histones deposited during S-Phase are often replaced by histone variants at discrete loci after replication. This function is facilitated by histone chaperones and chromatin remodeling complexes. The chromatin remodeler SWR1 incorporates H2A.Z into chromatin in exchange for its canonical counterpart H2A. Despite its importance, the mechanisms by which SWR1 is recruited to its target loci are not yet fully understood. Here, we show that ALFIN-LIKE (AL) proteins direct the SWR1 complex to H3K4me3 loci, facilitating the deposition of H2A.Z. Simultaneous mutation of the seven AL genes (al7m) leads to severe developmental effects and aberrant upregulation of responsive genes. This geneset exhibits high levels of H3K4me3, which is recognized by AL5. Furthermore, al7m shows a decrease in H2A.Z occupancy, particularly at AL5-bound loci. Our data suggests that AL5, through its interaction with SWR1, guides its activity towards inducible genes.

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Nucleosome free DNA- and acetyl histone-binding components recruit SWR1 to yeast promoters for H2A.Z replacement

Project description:The histone variant H2A.Z is a genome-wide signature of nucleosomes proximal to eukaryotic regulatory DNA. While the multi-subunit SWR1 chromatin remodeling complex is known to catalyze ATP-dependent deposition of H2A.Z, the mechanism of recruitment to S. cerevisiae promoters has been unclear. A sensitive assay for competitive binding of di-nucleosome substrates revealed that SWR1 preferentially binds long nucleosome-free DNA adjoining core particles, allowing discrimination of gene promoters over gene bodies. We traced the critical DNA binding component of SWR1 to the conserved Swc2/YL1 subunit, whose activity is required for both SWR1 binding and H2A.Z incorporation in vivo. Histone acetylation by NuA4 enhances SWR1 binding, but the interaction with nucleosome-free DNA is the major determinant. ‘Hierarchical cooperation’ between high affinity DNA- and low affinity histone modification-binding factors may reconcile the large disparity in affinities for chromatin substrates, and unify classical control by DNA-binding factors with post-translational histone modifications and ATP-dependent nucleosome mobility. Swr1 TAP IF of various mutants

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