A Topological Interaction between Cohesin Rings and a Circular Minichromosome

Ivanov, Dmitri; Nasmyth, Kim

doi:10.1016/j.cell.2005.07.018

Cited by 189 publications

(202 citation statements)

References 34 publications

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“…The large ring-like structure of cohesin, and several other lines of evidence, including topological linkage of cohesin to circular DNA molecules (Ivanov and Nasmyth 2005) supports the attractive hypothesis that cohesin mediates cohesion by encircling both sister chromatids (Nasmyth 2005;Fig. 1b).…”

Section: Cohesinsupporting

confidence: 53%

Roles of the sister chromatid cohesion apparatus in gene expression, development, and human syndromes

2006

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The sister chromatid cohesion apparatus mediates physical pairing of duplicated chromosomes. This pairing is essential for appropriate distribution of chromosomes into the daughter cells upon cell division. Recent evidence shows that the cohesion apparatus, which is a significant structural component of chromosomes during interphase, also affects gene expression and development. The Cornelia de Lange (CdLS) and Roberts/SC phocomelia (RBS/SC) genetic syndromes in humans are caused by mutations affecting components of the cohesion apparatus. Studies in Drosophila suggest that effects on gene expression are most likely responsible for developmental alterations in CdLS. Effects on chromatid cohesion are apparent in RBS/SC syndrome, but data from yeast and Drosophila point to the likelihood that changes in expression of genes located in heterochromatin could contribute to the developmental deficits.

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Section: Cohesinsupporting

confidence: 53%

Roles of the sister chromatid cohesion apparatus in gene expression, development, and human syndromes

2006

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“…that cohesin binds chromosomes by a topological embrace. 33,34 Cohesin itself appears to play a rather passive role during fork passage, consistent with a model in which the replication fork passes through it. Since the inner diameter of the cohesin ring measures 35 nm, in principle it is wide enough to encircle two sister strands of DNA, even when they are packed into nucleosomes.…”

Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andmentioning

confidence: 60%

“…Since the inner diameter of the cohesin ring measures 35 nm, in principle it is wide enough to encircle two sister strands of DNA, even when they are packed into nucleosomes. 33,34 Occasionally, the replisome dissociates from stalled forks, causing fork collapse. Fork collapse often generates pathological recombination intermediates-like structures and DNA breaks.…”

Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andmentioning

confidence: 99%

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Ogiwara

Enomoto²,

Seki³

2007

Cell Cycle

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Previously published online as a Cell Cycle E-publication: http://www.landesbioscience.com/journals/cc/abstract.php?id=4130 KEy wOrdSIno80, Arp8, Ctf18, RFC, PCNA, cohesin, chromosome segregation/sister chromatid cohesion, chromatin remodeling, replication fork AcKnOwlEdgEMEnTSWe thank P. Hieter, A. Sugino, Y. Kawasaki, and M. Arisawa for strains, antibodies and plasmids used in this study. We thank all members of the Enomoto lab for their support. This work was supported by Grants-in-Aid for Scientific Research on Priority Areas from The Ministry of Education, Science, Sports and Culture of Japan. nOTESupplemental material can be found at: http://www.landesbioscience.com/supplement/ogiwaraCC6-9-sup.pdf AbSTrAcTHere we identify a defect in sister chromatid cohesion in the Saccharomyces serevisiae arp8 mutant, which impairs the chromatin remodeling activity of the INO80 complex, and we report the direct association of Ino80 with centromeres and cohesin-associated regions. In early S phase, Ino80 is recruited to replication forks along with Ctf18 and PCNA, both of which are involved in the establishment of sister chromatid cohesion. The arp8 mutation perturbs the association of Ctf18 and PCNA but not of cohesin with replication forks. We propose that the INO80 complex is required for the proper establishment of sister chromatid cohesion.

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“…Studies of cohesin using a tobacco etch virus-cleavable subunit have led to a model in which cohesin functions as a ring that embraces both sister chromatids Ivanov and Nasmyth, 2005). To determine whether condensin also functions as a ring, albeit within rather than between sister chromatids, we constructed a form of SMC2 that could be cleaved by PreScission protease at two balanced sites in the coiled-coil region.…”

Section: Topological Integrity Of the Smc2-smc4 Heterodimer Is Not Rementioning

confidence: 99%

“…We have also generated the first biologically active cleavable form of SMC2, allowing us to break the putative condensin complex ring in vitro and determine whether condensin might function in an analogous way to cohesin by topologically embracing DNA Ivanov and Nasmyth, 2005). These studies were performed in DT40 cells with a conditional knockout of the SMC2 gene, so that all phenotypes observed reflect the activity of a homogeneous mutant complex, with no background of the wild-type protein.…”

Section: Introductionmentioning

confidence: 99%

Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Hudson

Ohta

Freisinger

et al. 2008

MBoC

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We engineered mutants into residues of SMC2 to dissect the role of ATPase function in the condensin complex. These residues are predicted to be involved in ATP binding or hydrolysis and in the Q-loop, which is thought to act as a mediator of conformational changes induced by substrate binding. All the engineered ATPase mutations resulted in lethality when introduced into SMC2 null cells. We found that ATP binding, but not hydrolysis, is essential to allow stable condensin association with chromosomes. How SMC proteins bind and interact with DNA is still a major question. Cohesin may form a ring structure that topologically encircles DNA. We examined whether condensin behaves in an analogous way to its cohesin counterpart, and we have generated a cleavable form of biologically active condensin with PreScission protease sites engineered into the SMC2 protein. This has allowed us to demonstrate that topological integrity of the SMC2-SMC4 heterodimer is not necessary for the stability of the condensin complex in vitro or for its stable association with mitotic chromosomes. Thus, despite their similar molecular organization, condensin and cohesin exhibit fundamental differences in their structure and function.

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A Topological Interaction between Cohesin Rings and a Circular Minichromosome

Cited by 189 publications

References 34 publications

Roles of the sister chromatid cohesion apparatus in gene expression, development, and human syndromes

Roles of the sister chromatid cohesion apparatus in gene expression, development, and human syndromes

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

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