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Functional crosstalk between the cohesin loader and a chromatin remodeler

ABSTRACT: Functional crosstalk between the cohesin loader and a chromatin remodeler

PROVIDER: PRJNA811515 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18182103_1.fastq.gz	Fastqsanger.gz
	SRR18182103_2.fastq.gz	Fastqsanger.gz
	SRR18182104_1.fastq.gz	Fastqsanger.gz
	SRR18182104_2.fastq.gz	Fastqsanger.gz
	SRR18182105_1.fastq.gz	Fastqsanger.gz

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Functional crosstalk between the cohesin loader and chromatin remodelers

Project description:The cohesin complex has crucial roles in many structural and functional aspects of chromosomes including sister chromatid cohesion, genome organization, gene transcription and DNA repair. Cohesin recruitment onto chromosomes requires nucleosome free DNA and a specialized cohesin loader complex comprised of the Scc2 and Scc4 subunits. The cohesin loader, in addition to stimulating cohesin ATP hydrolysis and facilitating topological loading onto DNA, leads cohesin to chromatin receptors such as the RSC chromatin remodeling complex. Here, we explore the cohesin loader-RSC interaction and show that its Scc4 subunit contacts a conserved RSC ATPase motor module. The cohesin loader enhances RSC chromatin remodeling activity in vitro, as well as promoter nucleosome eviction in vivo. These findings provide insight into how the cohesin loader recognizes, as well as influences, the chromatin landscape, with implications for our understanding of human developmental disorders including Cornelia de Lange and Coffin-Siris syndromes.

2022-11-29 | PXD033446 | Pride

Functional crosstalk between the cohesin loader and a chromatin remodeler

Project description:The Scc2-Scc4 complex interacts with a conserved RSC ATPase motor module. The cohesin loader enhances RSC remodeling activity in vitro and promoter nucleosome eviction in vivo.

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A Structure-Based Mechanism for DNA Entry into the Cohesin Ring

Project description:The ring-shaped cohesin complex is thought to fulfil its roles in sister chromatid cohesion, genome stability and gene regulation by topologically encircling DNAs. The ring is formed by two Structural Maintenance of Chromosome (SMC) subunits, whose ATPase heads are linked by a kleisin subunit. Additional components, including the Mis4Scc2/NIPL cohesin loader, engage the kleisin. Here, we visualize a DNA gripping intermediate during cohesin loading onto DNA by cryo-electron microscopy. ATP-dependent head engagement creates an interaction surface onto which Mis4Scc2/NIPL clamps the DNA. We use biophysical tools to establish the order of events during cohesin loading. DNA first traverses an N-terminal kleisin gate that was opened by ATP binding and closed again as the loader locks the DNA. Ensuing ATP hydrolysis and head disengagement, assisted by Mis4Scc2/NIPL, will complete DNA entry. A conserved kleisin N-terminal tail guides the DNA on its trajectory to successful topological DNA entry into the cohesin ring.

2020-08-05 | PXD018600 | Pride

Crosslinking/mass spectrometry (CLMS) analysis of Cohesin complex

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A Role for Chromatin Remodeling in Cohesin Loading onto Chromosomes

Project description:The RSC chromatin remodeling complex recruits the cohesin loader Scc2-Scc4 by a direct protein interaction. Nucleosome-free DNA is the substrate for the cohesin loading reaction.

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Isw1 contributes to cohesin association with centromeres and pericentromeric regions

Project description:Cohesin is a highly conserved, multiprotein complex whose canonical function is to hold sister chromatids together to ensure accurate chromosome segregation. Cohesin association with chromatin relies on the separate Scc2-Scc4 complex that enables cohesin ring opening and topological entrapment of sister DNAs. Cohesin loading at centromeres also requires the CTF19 kinetochore subcomplex that recruits Scc2-Scc4, ensuring efficient and targeted cohesin binding. After loading at centromeres, cohesin rapidly translocates to neighboring pericentromeric regions. In an attempt to better understand how sister chromatid cohesion is regulated, we performed a proteomic screen in budding yeast that identified the Isw1 chromatin remodeler as a cohesin binding partner. We found that while cohesin can associate with both Isw1-containing complexes, ISW1a and ISW1b, however only ISW1a localizes to centromeres. There, ISW1a utilizes its chromatin remodeling activity to allow efficient translocation of cohesin loaded through CTF19 at centromeres to pericentromeres. Consistently, lack of Isw1 results in cohesin and cohesin loader retainment at CENs and periCENs. Interestingly, lack of Isw1 resulted in changes in the nucleosomal landscape at the CENs and pericentromeric regions, suggesting that chromatin organization may be a crucial determinant of cohesin loading. Finally, we provide evidence that the role of ISW1a at the CENs is to restrict the activity of the RSC complex. Taken together, our results support the notion of a key role of chromatin environment for cohesin functions.

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Cohesin occupancy and composition at enhancers and promoters are linked to DNA replication origin proximity in Drosophila

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Project description:In addition to its well-know function in chromosome segregation, increasing evidence implicates cohesin in the control of gene expression. It has been previously reported that inactivation of the cohesin loader Mis4 in G1-arrested cells leads to the dissociation of cohesin from chromatin. We exploited this experimental situation to ask whether this loss of cohesin would affect gene expression on a genome-wide scale. Three independent inoculates (biological replicates) of cells carrying either the thermosensitive mis4-367 or the wild-type mis4+ allele were grown at permissive temperature of 25C. Cells were G1-arrested by titrating out the Cdc10 transcription factor by overexpression of the C-terminal fragment of its binding partner Res1, and then shifted for 2 hours at 37C. Cells were harvested before and after the temperature shift to proceed to total RNA extraction.

2010-08-12 | E-GEOD-23602 | biostudies-arrayexpress

Roles of the Brca2 and Wapl complexes with Pds5 in sister chromatid cohesion, cohesin localization, and gene expression [ChIP-seq]

Project description:The Pds5, Wapl and Brca2 proteins were mapped by ChIP-seq, and the effects of their depletion on the binding of cohesin subunits and the Nipped-B cohesin loader were examined by ChIP-seq

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