The acetyltransferase Eco1 elicits cohesin dimerization during S phase
© 2020 Shi et al..
Cohesin is a DNA-associated protein complex that forms a tripartite ring controlling sister chromatid cohesion, chromosome segregation and organization, DNA replication, and gene expression. Sister chromatid cohesion is established by the protein acetyltransferase Eco1, which acetylates two conserved lysine residues on the cohesin subunit Smc3 and thereby ensures correct chromatid separation in yeast (Saccharomyces cerevisiae) and other eukaryotes. However, the consequence of Eco1-catalyzed cohesin acetylation is unknown, and the exact nature of the cohesive state of chromatids remains controversial. Here, we show that self-interactions of the cohesin subunits Scc1/Rad21 and Scc3 occur in a DNA replication-coupled manner in both yeast and human cells. Using cross-linking MS-based and in vivo disulfide cross-linking analyses of purified cohesin, we show that a subpopulation of cohesin may exist as dimers. Importantly, upon temperature-sensitive and auxin-induced degron-mediated Eco1 depletion, the cohesin-cohesin interactions became significantly compromised, whereas deleting either the deacetylase Hos1 or the Eco1 antagonist Wpl1/Rad61 increased cohesin dimer levels by ∼20%. These results indicate that cohesin dimerizes in the S phase and monomerizes in mitosis, processes that are controlled by Eco1, Wpl1, and Hos1 in the sister chromatid cohesion-dissolution cycle. These findings suggest that cohesin dimerization is controlled by the cohesion cycle and support the notion that a double-ring cohesin model operates in sister chromatid cohesion.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:295 |
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| Enthalten in: |
The Journal of biological chemistry - 295(2020), 22 vom: 29. Mai, Seite 7554-7565 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Shi, Di [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 24.12.2020 Date Revised 13.12.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1074/jbc.RA120.013102 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM308972325 |
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| 245 | 1 | 4 | |a The acetyltransferase Eco1 elicits cohesin dimerization during S phase |
| 264 | 1 | |c 2020 | |
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| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 24.12.2020 | ||
| 500 | |a Date Revised 13.12.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2020 Shi et al. | ||
| 520 | |a Cohesin is a DNA-associated protein complex that forms a tripartite ring controlling sister chromatid cohesion, chromosome segregation and organization, DNA replication, and gene expression. Sister chromatid cohesion is established by the protein acetyltransferase Eco1, which acetylates two conserved lysine residues on the cohesin subunit Smc3 and thereby ensures correct chromatid separation in yeast (Saccharomyces cerevisiae) and other eukaryotes. However, the consequence of Eco1-catalyzed cohesin acetylation is unknown, and the exact nature of the cohesive state of chromatids remains controversial. Here, we show that self-interactions of the cohesin subunits Scc1/Rad21 and Scc3 occur in a DNA replication-coupled manner in both yeast and human cells. Using cross-linking MS-based and in vivo disulfide cross-linking analyses of purified cohesin, we show that a subpopulation of cohesin may exist as dimers. Importantly, upon temperature-sensitive and auxin-induced degron-mediated Eco1 depletion, the cohesin-cohesin interactions became significantly compromised, whereas deleting either the deacetylase Hos1 or the Eco1 antagonist Wpl1/Rad61 increased cohesin dimer levels by ∼20%. These results indicate that cohesin dimerizes in the S phase and monomerizes in mitosis, processes that are controlled by Eco1, Wpl1, and Hos1 in the sister chromatid cohesion-dissolution cycle. These findings suggest that cohesin dimerization is controlled by the cohesion cycle and support the notion that a double-ring cohesin model operates in sister chromatid cohesion | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a DNA replication | |
| 650 | 4 | |a Eco1 | |
| 650 | 4 | |a acetylation | |
| 650 | 4 | |a acetyltransferase | |
| 650 | 4 | |a cell cycle | |
| 650 | 4 | |a chromatid cohesion | |
| 650 | 4 | |a cohesin | |
| 650 | 4 | |a dimerization | |
| 650 | 4 | |a double ring model | |
| 650 | 4 | |a protein acetylation | |
| 650 | 4 | |a self-interaction | |
| 650 | 7 | |a Cell Cycle Proteins |2 NLM | |
| 650 | 7 | |a Chromosomal Proteins, Non-Histone |2 NLM | |
| 650 | 7 | |a IRR1 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a MCD1 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a Nuclear Proteins |2 NLM | |
| 650 | 7 | |a RAD61 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a Saccharomyces cerevisiae Proteins |2 NLM | |
| 650 | 7 | |a Histone Demethylases |2 NLM | |
| 650 | 7 | |a EC 1.14.11.- |2 NLM | |
| 650 | 7 | |a Acetyltransferases |2 NLM | |
| 650 | 7 | |a EC 2.3.1.- |2 NLM | |
| 650 | 7 | |a ECO1 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a EC 2.3.1.- |2 NLM | |
| 650 | 7 | |a HOS1 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a EC 3.5.1.98 |2 NLM | |
| 700 | 1 | |a Zhao, Shuaijun |e verfasserin |4 aut | |
| 700 | 1 | |a Zuo, Mei-Qing |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Jingjing |e verfasserin |4 aut | |
| 700 | 1 | |a Hou, Wenya |e verfasserin |4 aut | |
| 700 | 1 | |a Dong, Meng-Qiu |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Qinhong |e verfasserin |4 aut | |
| 700 | 1 | |a Lou, Huiqiang |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The Journal of biological chemistry |d 1945 |g 295(2020), 22 vom: 29. Mai, Seite 7554-7565 |w (DE-627)NLM000004995 |x 1083-351X |7 nnns |
| 773 | 1 | 8 | |g volume:295 |g year:2020 |g number:22 |g day:29 |g month:05 |g pages:7554-7565 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1074/jbc.RA120.013102 |3 Volltext |
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