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Calibrated Smc3 ChIP-seq for wild type, smc3-2R, wpl1Δ and smc3-2R wpl1Δ strains arrested in meiotic prophase I

ABSTRACT: Genome binding/occupancy profiling of the cohesin subunit Smc3 by high throughput sequencing. S. pombe is included as the calibration genome.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE185020 | GEO | 2022/02/04

REPOSITORIES: GEO

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Calibrated Smc3 ChIP-seq for wild type, eco1-aa, wpl1-delta and eco1-aa wpl1-delta strains arrested in meiotic prophase I

Project description:Genome binding/occupancy profiling of the cohesin subunit Smc3 by high throughput sequencing. S. pombe is included as the calibration genome.

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Calibrated Smc3 ChIP-seq for wild type, smc3-2R, wpl1Δ and smc3-2R wpl1Δ strains arrested in meiotic prophase I

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Calibrated Scc1 ChIP-seq for wild type and rad61Δ strains arrested in metaphase with and without tension

Project description:Genome binding/occupancy profiling of the cohesin subunit Scc1 by high throughput sequencing. S. pombe is included as the calibration genome.

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Calibrated Scc1 ChIP-seq for wild type and chl4Δ strains arrested in metaphase with and without tension

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Calibrated Sgo1 and Brn1 ChIP-seq for wild type strains arrested in metaphase without tension

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Meiotic cohesins modulate chromosome compaction during meiotic prophase in fission yeast

Project description:The meiotic cohesin Rec8 is required for the stepwise segregation of chromosomes during the two rounds of meiotic division. By directly measuring chromosome compaction in living cells of the fission yeast Schizosaccharomyces pombe, we found an additional role for the meiotic cohesin in the compaction of chromosomes during meiotic prophase. In the absence of Rec8, chromosomes were decompacted relative to those of wild-type cells. Conversely, loss of the cohesin-associated protein Pds5 resulted in hyper-compaction. While this hyper-compaction requires Rec8, binding of Rec8 to chromatin was reduced in the absence of Pds5, indicating that Pds5 promotes chromosome association of Rec8. To explain these observations, we propose that meiotic prophase chromosomes are organized as chromatin loops emanating from a Rec8-containing axis; the absence of Rec8 disrupts the axis, resulting in disorganized chromosomes, whereas reduced Rec8 loading results in a longitudinally compacted axis with fewer attachment points and longer chromatin loops. Keywords: ChIP-chip analysis ChIP analysis of Rec8: In all cases, hybridization data for ChIP fraction was compared with that of SUP (supernatant) fraction. Pombe chromosome II, III array was used.

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The Smc3 deacetylase Hos1 closes the cohesin acetylation cycle

Project description:Cohesion between sister chromatids is mediated by the chromosomal cohesin complex. In budding yeast, cohesin is loaded onto chromosomes during the G1 phase of the cell cycle. During S-phase, the replication fork-associated acetyltransferase Eco1 acetylates the cohesin subunit Smc3 to promote establishment of sister chromatid cohesion. At the time of anaphase, Smc3 loses its acetylation again, but the Smc3 deacetylase and possible importance of Smc3 deacetylation are unknown. Here, we show that the class I histone deacetylase family member Hos1 is responsible for Smc3 deacetylation. Cohesin is protected from deacetylation while bound to chromosomes, but is deacetylated as soon as it dissociates from chromosomes following separase cleavage at anaphase onset. Non-acetylated Smc3 is required as a substrate for cohesion establishment in the following cell cycle. Our results complete the description of the Smc3 acetylation cycle and provide unexpected insight into the importance of de novo Smc3 acetylation for cohesion establishment.

2010-06-10 | GSE22257 | GEO

Meiotic cohesins modulate chromosome compaction during meiotic prophase in fission yeast

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Conformational dynamics of cohesin/Scc2 loading complex are regulated by Smc3 acetylation and ATP association

Project description:The ring-shaped cohesin complex is the key player in sister chromatid cohesion, DNA repair, and gene transcription. The loading of cohesin to chromosomes requires the loader Scc2 and is regulated by ATP. This process is also hindered by Smc3 acetylation. However, the molecular mechanism behind this inhibition remains mysterious. Here we identify a novel configuration of Scc2 with pre-engaged cohesin and reveal dynamic conformations of the cohesin/Scc2 complex in the loading reaction. We demonstrate that Smc3 acetylation blocks the association of Scc2 with pre-engaged cohesin by impairing the interaction of Scc2 with Smc3’s head. Lastly, we show that ATP binding induces the cohesin/Scc2 complex to clamp DNA by promoting the interaction between Scc2 and Smc3 coiled-coil. Our results illuminate a dynamic reconfiguration of the cohesin/Scc2 complex during loading and indicate how Smc3 acetylation and ATP regulate this process.

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