Smc3 Deacetylation by Hos1 Facilitates Efficient Dissolution of Sister Chromatid Cohesion during Early Anaphase

Li, Shuyu; Yue, Zuojun; Tanaka, Tomoyuki

doi:10.1016/j.molcel.2017.10.009

Cited by 24 publications

(21 citation statements)

References 38 publications

(93 reference statements)

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“…The finding that acetylation of Smc3 during S phase is accompanied by a pronounced increase in J but decrease in E suggests that entrapment of sister DNAs within J-K compartments may be a feature of cohesion throughout the genome and does not merely apply to small circular minichromosomes. The observation that sister DNAs are entrapped in J-K compartments refines our view of cohesion while the failure to observe entrapment exclusively by open SK rings, S compartments, E-K compartments, or entrapment of one DNA in an S and its sister in a K compartment exclude most previously proposed scenarios Li et al, 2017;Murayama et al, 2018;Murayama and Uhlmann, 2015). It is nevertheless important to point out that detection of sister DNA entrapment by J-K compartments does not exclude the possibility that J-K compartments are in dynamic equilibrium with open SK rings.…”

Section: Discussionsupporting

confidence: 66%

“…Thus, the observation that DNAs are entrapped by J-K compartments does not exclude the possibility that transient dissociation of Smc heads gives rise to open SK rings that would also maintain entrapment. Indeed, the notion that J-K compartments are in a dynamic equilibrium with open SK rings is the simplest way of explaining how cleavage of Smc3 coiled coils is sufficient to release cohesin from DNA Li et al, 2017;Murayama and Uhlmann, 2015).…”

Section: Sister Dnas Are Entrapped Within J-k Compartmentsmentioning

confidence: 99%

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The topology of DNA entrapment by cohesin rings

Chapard

Jones

et al. 2018

Preprint

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Cohesin entraps sister DNAs within tripartite rings created by pairwise interactions between Smc1, Smc3, and Scc1. Because the ATPase heads of Smc1 and Smc3 can interact with each other, cohesin rings in fact have the potential to form a variety of sub-compartments. Using in vivo cysteine crosslinking, we show that when Smc1 and Smc3 ATPases are engaged in the presence of ATP (E heads) cohesin rings generate a "SMC (S) compartment" between hinge and E heads and a "kleisin (K) compartment" between E heads and their associated kleisin subunit. Upon ATP hydrolysis, cohesin's heads associate with each other in a very different mode, in which their signature motifs and their coiled coils are closely juxtaposed (J heads), creating alternative S and K compartments. We show that all four sub-compartments exist in vivo, that acetylation of Smc3 during S phase is accompanied by an increase in the ratio of J to E heads, and that sister DNAs are entrapped in J-K but not E-K compartments or in either type of S compartment.

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Section: Discussionsupporting

confidence: 66%

Section: Sister Dnas Are Entrapped Within J-k Compartmentsmentioning

confidence: 99%

The topology of DNA entrapment by cohesin rings

Chapard

Jones

et al. 2018

Preprint

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“…Cells were cultured at 25ºC in YPA medium containing 2% glucose (YPAD) unless otherwise stated. Constructs of GAL1-10 promoter-CEN3-tetOs [26, 43,44], TetR-3×CFP [43,45], MET3 promoter-CDC20 [46], mCherry-TUB1 [47], SPC42-4×mCherry, NIC96-4×mCherry [48], CEN2-tetOs (tetO×224 was inserted 600 bp away from CEN2) [20] and tetOs at 15 kb from CEN12 [20] were described previously. To generate bir1∆ and mcm21∆, the whole coding region of the gene was replaced with the Kl.…”

Section: Yeast Strains and Cell Culturementioning

confidence: 99%

Aurora B-INCENP localization at centromeres/inner kinetochores is essential for chromosome bi-orientation in budding yeast

García-Rodríguez

Kasciukovic

Denninger

et al. 2019

Preprint

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To promote chromosome bi-orientation, Aurora B kinase weakens and disrupts aberrant kinetochore-MT interaction. It has long been debated how Aurora B halts this action when biorientation is established and tension is applied across sister kinetochores. Pertinent to this debate, it was shown that Bir1 (yeast Survivin), which recruits Ipl1-Sli15 (yeast Aurora B-INCENP) to centromeres, is dispensable for bi-orientation, raising the possibility that Aurora B localization at centromeres is not required for bi-orientation. Here, we show that the COMA inner kinetochore sub-complex physically interacts with Sli15, recruits Ipl1-Sli15 to the inner kinetochore and promotes chromosome bi-orientation, independently of Bir1, in budding yeast. Moreover, using an engineered recruitment of Ipl1-Sli15 to the inner kinetochore when both Bir1 and COMA are defective, we show that localization of Ipl1-Sli15 at centromeres/ inner kinetochores is essential for bi-orientation, refuting the above possibility. Our results give important insight into how Aurora B disrupts kinetochore-MT interaction in a tensiondependent manner, to promote chromosome bi-orientation. (164 words)

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“…At the same time, the centromeric cohesin is protected by the Sgo1-PP2A (shugoshin 1-protein phosphatase 2A) complex and Haspin (histone H3-associated protein kinase) until metaphase [9, 10]. The cleavage of Rad21 by separase and the deacetylation of Smc3 by histone deacetylase Hdac8 at the metaphase–anaphase transition promote the complete removal of cohesin from chromatin [11–13]. This precise regulation of the cohesin complex ensures the accurate chromosome segregation in cell cycle progression.…”

Section: Introductionmentioning

confidence: 99%

NudCL2 is an Hsp90 cochaperone to regulate sister chromatid cohesion by stabilizing cohesin subunits

Yang¹,

Wang²,

Li³

et al. 2018

Cell. Mol. Life Sci.

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Sister chromatid cohesion plays a key role in ensuring precise chromosome segregation during mitosis, which is mediated by the multisubunit cohesin complex. However, the molecular regulation of cohesin subunits stability remains unclear. Here, we show that NudCL2 (NudC-like protein 2) is essential for the stability of cohesin subunits by regulating Hsp90 ATPase activity in mammalian cells. Depletion of NudCL2 induces mitotic defects and premature sister chromatid separation and destabilizes cohesin subunits that interact with NudCL2. Similar defects are also observed upon inhibition of Hsp90 ATPase activity. Interestingly, ectopic expression of Hsp90 efficiently rescues the protein instability and functional deficiency of cohesin induced by NudCL2 depletion, but not vice versa. Moreover, NudCL2 not only binds to Hsp90, but also significantly modulates Hsp90 ATPase activity and promotes the chaperone function of Hsp90. Taken together, these data suggest that NudCL2 is a previously undescribed Hsp90 cochaperone to modulate sister chromatid cohesion by stabilizing cohesin subunits, providing a hitherto unrecognized mechanism that is crucial for faithful chromosome segregation during mitosis.Electronic supplementary materialThe online version of this article (10.1007/s00018-018-2957-y) contains supplementary material, which is available to authorized users.

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Smc3 Deacetylation by Hos1 Facilitates Efficient Dissolution of Sister Chromatid Cohesion during Early Anaphase

Cited by 24 publications

References 38 publications

The topology of DNA entrapment by cohesin rings

The topology of DNA entrapment by cohesin rings

Aurora B-INCENP localization at centromeres/inner kinetochores is essential for chromosome bi-orientation in budding yeast

NudCL2 is an Hsp90 cochaperone to regulate sister chromatid cohesion by stabilizing cohesin subunits

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