Condensin positioning at telomeres by shelterin proteins drives sister-telomere disjunction in anaphase

Colin, Léonard; Reyes, Céline; Berthezene, Julien; Maestroni, Laetitia; Modolo, Laurent; Toselli, Esther; Chanard, Nicolas; Schaak, Stéphane; Cuvier, Olivier; Gachet, Yannick; Coulon, Stéphane; Bernard, Pascal; Tournier, Sylvie

doi:10.1101/2022.03.18.484892

Cited by 4 publications

(7 citation statements)

References 86 publications

(176 reference statements)

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“…S1B ). These data are in agreement with previous reports of condensin enrichment at the border of telomeres in budding yeast, fission yeast, and vertebrates during mitosis 46–48 .…”

Section: Mainsupporting

confidence: 93%

Telomere protein arrays stall DNA loop extrusion by condensin

Analikwu,

Deshayes,

van der Torre

et al. 2023

Preprint

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DNA loop extrusion by SMC proteins is a key process underlying chromosomal organization. It is unknown how loop extruders interact with telomeres where chromosome ends are covered with a dense array of tens of neighboring DNA-binding proteins. Using complementaryin vivoandin vitrosingle-molecule approaches, we study the interaction between loop-extruding condensin and arrays of Rap1, the double-stranded-DNA-binding telomeric protein ofSaccharomyces cerevisiae. We show that dense linear Rap1 arrays can completely halt DNA loop extrusion, where the blocking efficiency depends on the array length and the DNA gap size between neighboring proteins. In cells, Rap1 arrays in the chromosome are found to act as contact insulators and to accumulate condensin at their borders, with direct implications for the resolution of dicentric chromosomes produced by telomere fusions. Our findings show that linear arrays of DNA-bound proteins can efficiently halt DNA loop extrusion by SMC proteins, which may impact a wide range of cellular processes from telomere functions to transcription and DNA repair.

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“…S1B ). These data are in agreement with previous reports of condensin enrichment at the border of telomeres in budding yeast, fission yeast, and vertebrates during mitosis 46–48 .…”

Section: Mainsupporting

confidence: 93%

Telomere protein arrays stall DNA loop extrusion by condensin

Analikwu,

Deshayes,

van der Torre

et al. 2023

Preprint

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“…The deduplicated bam files were converted to bigwig and bedgraph formats using deepTools (3.5.1). Normalization and generation of ratio coverage files were generated using software and scripts contained in the docker containers lbmc/chip_quant_r:0.0.6 and biocontainers/danpos:v2.2.2_cv3 ( Colin et al, 2022 Preprint ).…”

Section: Methodsmentioning

confidence: 99%

Dispersal of PRC1 condensates disrupts polycomb chromatin domains and loops

Williamson¹,

Boyle²,

Friman³

et al. 2023

Life Sci. Alliance

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Polycomb repressive complex 1 (PRC1) strongly influences 3D genome organization, mediating local chromatin compaction and clustering of target loci. Several PRC1 subunits have the capacity to form biomolecular condensates through liquid–liquid phase separation in vitro and when tagged and over-expressed in cells. Here, we use 1,6-hexanediol, which can disrupt liquid-like condensates, to examine the role of endogenous PRC1 biomolecular condensates on local and chromosome-wide clustering of PRC1-bound loci. Using imaging and chromatin immunoprecipitation, we show that PRC1-mediated chromatin compaction and clustering of targeted genomic loci—at different length scales—can be reversibly disrupted by the addition and subsequent removal of 1,6-hexanediol to mouse embryonic stem cells. Decompaction and dispersal of polycomb domains and clusters cannot be solely attributable to reduced PRC1 occupancy detected by chromatin immunoprecipitation following 1,6-hexanediol treatment as the addition of 2,5-hexanediol has similar effects on binding despite this alcohol not perturbing PRC1-mediated 3D clustering, at least at the sub-megabase and megabase scales. These results suggest that weak hydrophobic interactions between PRC1 molecules may have a role in polycomb-mediated genome organization.

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“…In unpublished work, we have identified CENP-I as part of the M18BP1 receptor at kinetochores (KW, DP, and AM, unpublished results). In addition, many other regulators such as transcription factors, histones, various histone modifications, protein phosphatase 2A (PP2A), Shugoshin, and telomeric proteins have been proposed to contribute to chromosome recruitment of condensin II 13, [51][52][53][54][55][56][57][58][59][60][61] . Whether these determinants are linked to the function of M18BP1 is currently unclear and grants future analyses.…”

Section: A Moonlighting Role For M18bp1mentioning

confidence: 99%

Condensin II activation by M18BP1

Borsellini,

Conti,

Cutts

et al. 2024

Preprint

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Condensin complexes promote the drastic spatial rearrangement of the genome upon mitotic entry. Condensin II initiates chromosome condensation in early mitosis. To prevent chromosome condensation during interphase, condensin II is inhibited by MCPH1, but the mechanism is unknown. Through genetic and proteomic approaches, we identify M18BP1, a protein previously associated with centromere identity, as a factor required for condensin II localization to chromatin. M18BP1 directly binds condensin II's CAP-G2 subunit and competes with MCPH1 for binding. Upon mitotic entry, CDK1 mediated phosphorylation may promote a switch from MCPH1 to M18BP1 binding to activate condensin II. Our results identify a fundamental and evolutionarily conserved mechanism of condensin II activation.

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Condensin positioning at telomeres by shelterin proteins drives sister-telomere disjunction in anaphase

Cited by 4 publications

References 86 publications

Telomere protein arrays stall DNA loop extrusion by condensin

Telomere protein arrays stall DNA loop extrusion by condensin

Dispersal of PRC1 condensates disrupts polycomb chromatin domains and loops

Condensin II activation by M18BP1

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