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Article ; Online: The magic and meaning of Mendel's miracle.

Nasmyth, Kim

2022 Volume 23, Issue 7, Page(s) 447–452

Abstract: July 2022 will see the bicentenary of the birth of Gregor Mendel, often hailed as the 'father of modern genetics'. To mark the occasion, I retrace Mendel's origins, revisit his famous study 'Experiments in plant hybridization', and reflect on the ... ...

Abstract	July 2022 will see the bicentenary of the birth of Gregor Mendel, often hailed as the 'father of modern genetics'. To mark the occasion, I retrace Mendel's origins, revisit his famous study 'Experiments in plant hybridization', and reflect on the revolutionary implications of his work and scientific legacy that continues to shape modern biomedicine to this day.
Language	English
Publishing date	2022-05-20
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2035157-4
ISSN	1471-0064 ; 1471-0056
ISSN (online)	1471-0064
ISSN	1471-0056
DOI	10.1038/s41576-022-00497-2
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Article ; Online: How are DNAs woven into chromosomes?

Nasmyth, Kim

Science (New York, N.Y.)

2018 Volume 358, Issue 6363, Page(s) 589–590

MeSH term(s)	Chromosomes ; DNA/genetics ; Humans
Chemical Substances	DNA (9007-49-2)
Language	English
Publishing date	2018-01-03
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aap8729
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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: DNA passes through cohesin's hinge as well as its Smc3-kleisin interface.

Collier, James E / Nasmyth, Kim A

eLife

2022 Volume 11

Abstract: The ring model proposes that sister chromatid cohesion is mediated by co-entrapment of sister DNAs inside a single tripartite cohesin ring. The model explains how Scc1 cleavage triggers anaphase but has hitherto only been rigorously tested using small ... ...

Abstract	The ring model proposes that sister chromatid cohesion is mediated by co-entrapment of sister DNAs inside a single tripartite cohesin ring. The model explains how Scc1 cleavage triggers anaphase but has hitherto only been rigorously tested using small circular mini-chromosomes in yeast, where covalently circularizing the ring by crosslinking its three interfaces induces catenation of individual and sister DNAs. If the model applies to real chromatids, then the ring must have a DNA entry gate essential for mitosis. Whether this is situated at the Smc3/Scc1 or Smc1/Smc3 hinge interface is an open question. We have previously demonstrated DNA entrapment by cohesin in vitro (Collier et al., 2020). Here we show that cohesin in fact possesses two DNA gates, one at the Smc3/Scc1 interface and a second at the Smc1/3 hinge. Unlike the Smc3/Scc1 interface, passage of DNAs through SMC hinges depends on both Scc2 and Scc3, a pair of regulatory subunits necessary for entrapment in vivo. This property together with the lethality caused by locking this interface but not that between Smc3 and Scc1 in vivo suggests that passage of DNAs through the hinge is essential for building sister chromatid cohesion. Passage of DNAs through the Smc3/Scc1 interface is necessary for cohesin's separase-independent release from chromosomes and may therefore largely serve as an exit gate.
MeSH term(s)	Cell Cycle Proteins/genetics ; Chromatids ; Chromosomal Proteins, Non-Histone/genetics ; DNA ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; SCC2 protein, S cerevisiae ; SMC3 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2022-09-12
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.80310
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Article ; Online: What AlphaFold tells us about cohesin's retention on and release from chromosomes.

Nasmyth, Kim A / Lee, Byung-Gil / Roig, Maurici Brunet / Löwe, Jan

eLife

2023 Volume 12

Abstract: Cohesin is a trimeric complex containing a pair of SMC proteins (Smc1 and Smc3) whose ATPase domains at the end of long coiled coils (CC) are interconnected by Scc1. During interphase, it organizes chromosomal DNA topology by extruding loops in a manner ... ...

Abstract	Cohesin is a trimeric complex containing a pair of SMC proteins (Smc1 and Smc3) whose ATPase domains at the end of long coiled coils (CC) are interconnected by Scc1. During interphase, it organizes chromosomal DNA topology by extruding loops in a manner dependent on Scc1's association with two large hook-shaped proteins called SA (yeast: Scc3) and Nipbl (Scc2). The latter's replacement by Pds5 recruits Wapl, which induces release from chromatin via a process requiring dissociation of Scc1's N-terminal domain (NTD) from Smc3. If blocked by Esco (Eco)-mediated Smc3 acetylation, cohesin containing Pds5 merely maintains pre-existing loops, but a third fate occurs during DNA replication, when Pds5-containing cohesin associates with Sororin and forms structures that hold sister DNAs together. How Wapl induces and Sororin blocks release has hitherto remained mysterious. In the 20 years since their discovery, not a single testable hypothesis has been proposed as to their role. Here, AlphaFold 2 (AF) three-dimensional protein structure predictions lead us to propose formation of a quarternary complex between Wapl, SA, Pds5, and Scc1's NTD, in which the latter is juxtaposed with (and subsequently sequestered by) a highly conserved cleft within Wapl's C-terminal domain. AF also reveals how Scc1's dissociation from Smc3 arises from a distortion of Smc3's CC induced by engagement of SMC ATPase domains, how Esco acetyl transferases are recruited to Smc3 by Pds5, and how Sororin prevents release by binding to the Smc3/Scc1 interface. Our hypotheses explain the phenotypes of numerous existing mutations and are highly testable.
MeSH term(s)	Saccharomyces cerevisiae Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Chromosomes/metabolism ; Saccharomyces cerevisiae/genetics ; DNA/metabolism ; Adenosine Triphosphatases/metabolism ; Chromatids/metabolism ; Cohesins
Chemical Substances	Saccharomyces cerevisiae Proteins ; Cell Cycle Proteins ; DNA (9007-49-2) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2023-11-17
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.88656
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Article ; Online: A meiotic mystery: How sister kinetochores avoid being pulled in opposite directions during the first division.

Nasmyth, Kim

BioEssays : news and reviews in molecular, cellular and developmental biology

2015 Volume 37, Issue 6, Page(s) 657–665

Abstract: We now take for granted that despite the disproportionate contribution of females to initial growth of their progeny, there is little or no asymmetry in the contribution of males and females to the eventual character of their shared offspring. In fact, ... ...

Abstract	We now take for granted that despite the disproportionate contribution of females to initial growth of their progeny, there is little or no asymmetry in the contribution of males and females to the eventual character of their shared offspring. In fact, this key insight was only established towards the end of the eighteenth century by Joseph Koelreuter's pioneering plant breeding experiments. If males and females supply equal amounts of hereditary material, then the latter must double each time an embryo is conceived. How then does the amount of this mysterious stuff not multiply exponentially from generation to generation? A compensatory mechanism for diluting the hereditary material must exist, one that ensures that if each parent contributes one half, each grandparent contributes a quarter, and each great grandparent merely an eighth. An important piece of the puzzle of how hereditary material is diluted at each generation has been elucidated over the past ten years.
MeSH term(s)	Animals ; Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/physiology ; Cell Division ; Chromosome Segregation ; Humans ; Kinetochores/physiology ; Meiosis ; Mitosis ; Protein Serine-Threonine Kinases/physiology ; Proto-Oncogene Proteins/physiology ; Saccharomyces cerevisiae Proteins/physiology ; Polo-Like Kinase 1
Chemical Substances	Cell Cycle Proteins ; Proto-Oncogene Proteins ; REC8 protein, human ; Saccharomyces cerevisiae Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; CDC5 protein, S cerevisiae (EC 2.7.11.21)
Language	English
Publishing date	2015-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201500006
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Article ; Online: Sister chromatid cohesion establishment during DNA replication termination.

Cameron, George / Gruszka, Dominika T / Gruar, Rhian / Xie, Sherry / Kaya, Çağla / Nasmyth, Kim A / Baxter, Jonathan / Srinivasan, Madhusudhan / Yardimci, Hasan

Science (New York, N.Y.)

2024 Volume 384, Issue 6691, Page(s) 119–124

Abstract: Newly copied sister chromatids are tethered together by the cohesin complex, but how sister chromatid cohesion coordinates with DNA replication is poorly understood. Prevailing models suggest that cohesin complexes, bound to DNA before replication, ... ...

Abstract	Newly copied sister chromatids are tethered together by the cohesin complex, but how sister chromatid cohesion coordinates with DNA replication is poorly understood. Prevailing models suggest that cohesin complexes, bound to DNA before replication, remain behind the advancing replication fork to keep sister chromatids together. By visualizing single replication forks colliding with preloaded cohesin complexes, we find that the replisome instead pushes cohesin to where a converging replisome is met. Whereas the converging replisomes are removed during DNA replication termination, cohesin remains on nascent DNA and provides cohesion. Additionally, we show that CMG (CDC45-MCM2-7-GINS) helicase disassembly during replication termination is vital for proper cohesion in budding yeast. Together, our results support a model wherein sister chromatid cohesion is established during DNA replication termination.
MeSH term(s)	Chromatids/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Cohesins/metabolism ; DNA Replication ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sister Chromatid Exchange ; Minichromosome Maintenance Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Nuclear Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; Cohesins ; Saccharomyces cerevisiae Proteins ; CDC45 protein, S cerevisiae ; Minichromosome Maintenance Proteins (EC 3.6.4.12) ; DNA-Binding Proteins ; Nuclear Proteins
Language	English
Publishing date	2024-03-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.adf0224
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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Cohesin: a catenase with separate entry and exit gates?

Nasmyth, Kim

Nature cell biology

2011 Volume 13, Issue 10, Page(s) 1170–1177

Abstract: Cohesin confers both intrachromatid and interchromatid cohesion through formation of a tripartite ring within which DNA is thought to be entrapped. Here, I discuss what is known about the four stages of the cohesin ring cycle using the ring model as an ... ...

Abstract	Cohesin confers both intrachromatid and interchromatid cohesion through formation of a tripartite ring within which DNA is thought to be entrapped. Here, I discuss what is known about the four stages of the cohesin ring cycle using the ring model as an intellectual framework. I postulate that cohesin loading onto chromosomes, catalysed by a separate complex called kollerin, is mediated by the entry of DNA into cohesin rings, whereas dissociation, catalysed by Wapl and several other cohesin subunits (an activity that will be called releasin here), is mediated by the subsequent exit of DNA. I suggest that the ring's entry and exit gates may be separate, with the former and latter taking place at Smc1-Smc3 and Smc3-kleisin interfaces, respectively. Establishment of cohesion during S phase involves neutralization of releasin through acetylation of Smc3 at a site close to the putative exit gate of DNA, which locks rings shut until opened irreversibly by kleisin cleavage through the action of separase, an event that triggers the metaphase to anaphase transition.
MeSH term(s)	Animals ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes/enzymology ; Chromosomes/metabolism ; DNA/metabolism ; Humans ; Mitosis ; Models, Genetic ; Signal Transduction ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; DNA (9007-49-2)
Language	English
Publishing date	2011-10-03
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb2349
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Conformational dynamics of cohesin/Scc2 loading complex are regulated by Smc3 acetylation and ATP binding.

Kaushik, Aditi / Than, Thane / Petela, Naomi J / Voulgaris, Menelaos / Percival, Charlotte / Daniels, Peter / Rafferty, John B / Nasmyth, Kim A / Hu, Bin

Nature communications

2023 Volume 14, Issue 1, Page(s) 5929

Abstract: The ring-shaped cohesin complex is a 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 hindered by Smc3 acetylation. ... ...

Abstract	The ring-shaped cohesin complex is a 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 hindered by Smc3 acetylation. However, the molecular mechanism underlying this inhibition remains mysterious. Here, using Saccharomyces cerevisiae as a model system, 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.
MeSH term(s)	Acetylation ; Adenosine Triphosphate ; Cell Nucleus ; Molecular Conformation ; Saccharomyces cerevisiae/genetics ; Cohesins
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE) ; SCC2 protein, S cerevisiae ; SMC3 protein, S cerevisiae
Language	English
Publishing date	2023-09-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-41596-w
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Article ; Online: How far will we see in the future?

Nasmyth, Kim

Molecular biology of the cell

2010 Volume 21, Issue 22, Page(s) 3813–3814

MeSH term(s)	Cell Biology/trends ; Cell Division/genetics ; Eukaryotic Cells/cytology ; Eukaryotic Cells/metabolism ; Forecasting ; Molecular Biology/methods ; Molecular Biology/trends ; Prokaryotic Cells/cytology ; Prokaryotic Cells/metabolism
Language	English
Publishing date	2010-11-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E10-04-0359
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Sister chromatid cohesion is mediated by individual cohesin complexes.

Ochs, Fena / Green, Charlotte / Szczurek, Aleksander Tomasz / Pytowski, Lior / Kolesnikova, Sofia / Brown, Jill / Gerlich, Daniel Wolfram / Buckle, Veronica / Schermelleh, Lothar / Nasmyth, Kim Ashley

Science (New York, N.Y.)

2024 Volume 383, Issue 6687, Page(s) 1122–1130

Abstract: Eukaryotic genomes are organized by loop extrusion and sister chromatid cohesion, both mediated by the multimeric cohesin protein complex. Understanding how cohesin holds sister DNAs together, and how loss of cohesion causes age-related infertility in ... ...

Abstract	Eukaryotic genomes are organized by loop extrusion and sister chromatid cohesion, both mediated by the multimeric cohesin protein complex. Understanding how cohesin holds sister DNAs together, and how loss of cohesion causes age-related infertility in females, requires knowledge as to cohesin's stoichiometry in vivo. Using quantitative super-resolution imaging, we identified two discrete populations of chromatin-bound cohesin in postreplicative human cells. Whereas most complexes appear dimeric, cohesin that localized to sites of sister chromatid cohesion and associated with sororin was exclusively monomeric. The monomeric stoichiometry of sororin:cohesin complexes demonstrates that sister chromatid cohesion is conferred by individual cohesin rings, a key prediction of the proposal that cohesion arises from the co-entrapment of sister DNAs.
MeSH term(s)	Humans ; Cell Cycle Proteins/metabolism ; Chromatids/metabolism ; Chromatin/metabolism ; Cohesins/metabolism ; DNA/genetics ; DNA/metabolism ; Sister Chromatid Exchange ; Cell Line, Tumor
Chemical Substances	Cell Cycle Proteins ; Chromatin ; Cohesins ; DNA (9007-49-2) ; CDCA5 protein, human
Language	English
Publishing date	2024-03-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.adl4606
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