Molecular Architecture of SMC Proteins and the Yeast Cohesin Complex

Haering, Christian H.; Löwe, Jan; Hochwagen, Andreas; Nasmyth, Kim

doi:10.1016/s1097-2765(02)00515-4

Cited by 669 publications

(935 citation statements)

References 35 publications

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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 Andsupporting

confidence: 79%

“…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%

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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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Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andsupporting

confidence: 79%

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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“…SMC proteins contain N-and Cterminal nucleotide-binding motifs, called Walker A and B domains, separated by an extensive coiled-coil region that contains a central hinge (Hirano, 2002;Jessberger, 2003). The hinge allows SMC proteins to fold back on themselves, forming an intramolecular coiled-coil and creating an ATPase by juxtaposing the Walker A and B domains (Haering et al, 2002). SMC proteins form stable heterodimers, most likely through interactions mediated by their hinge regions (Haering et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…The hinge allows SMC proteins to fold back on themselves, forming an intramolecular coiled-coil and creating an ATPase by juxtaposing the Walker A and B domains (Haering et al, 2002). SMC proteins form stable heterodimers, most likely through interactions mediated by their hinge regions (Haering et al, 2002).Hypomorphic mutations of proteins in the SMC complexes render cells hypersensitive to genotoxic stress (Birkenbihl and Subramani, 1992;Lehmann et al, 1995;Sjogren and Nasmyth, 2001;Aono et al, 2002;Fujioka et al, 2002;Kim et al, 2002b;Yazdi et al, 2002;McDonald et al, 2003;Harvey et al, 2004). Cohesin may facilitate the homologous recombination repair of DSBs by holding sister-chromatids in proximity, promoting identification of an intact homologous duplex.…”

mentioning

confidence: 99%

“…Mutants of these non-SMC subunits display phenotypes very similar to those of the SMC mutants, consistent with their interdependent functions. Budding yeast cohesin subunit SCC1 controls the association of cohesin with chromosomes, perhaps by closing a loop-shaped complex via interactions with both head groups of SMC1ϩ3, which can encircle chromosomes (Haering et al, 2002;Jessberger, 2003). At mitosis, separase (ESP1) cleaves SCC1, thus abrogating the cohesin loop structure and sister chromatid cohesion.…”

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confidence: 99%

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Nse1, Nse2, and a Novel Subunit of the Smc5-Smc6 Complex, Nse3, Play a Crucial Role in Meiosis

Pébernard

McDonald

Pavlova

et al. 2004

MBoC

113

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The structural maintenance of chromosomes (SMC) family of proteins play key roles in the organization, packaging, and repair of chromosomes. Cohesin (Smc1؉3) holds replicated sister chromatids together until mitosis, condensin (Smc2؉4) acts in chromosome condensation, and Smc5؉6 performs currently enigmatic roles in DNA repair and chromatin structure. The SMC heterodimers must associate with non-SMC subunits to perform their functions. Using both biochemical and genetic methods, we have isolated a novel subunit of the Smc5؉6 complex, Nse3. Nse3 is an essential nuclear protein that is required for normal mitotic chromosome segregation and cellular resistance to a number of genotoxic agents. Epistasis with Rhp51 (Rad51) suggests that like Smc5؉6, Nse3 functions in the homologous recombination based repair of DNA damage. We previously identified two non-SMC subunits of Smc5؉6 called Nse1 and Nse2. Analysis of nse1-1, nse2-1, and nse3-1 mutants demonstrates that they are crucial for meiosis. The Nse1 mutant displays meiotic DNA segregation and homologous recombination defects. Spore viability is reduced by nse2-1 and nse3-1, without affecting interhomolog recombination. Finally, genetic interactions shared by the nse mutants suggest that the Smc5؉6 complex is important for replication fork stability. INTRODUCTIONBoth endogenous and exogenous agents constantly threaten genomic integrity. The DNA double-strand break (DSB) is a potentially life-threatening lesion for a cell and can occur spontaneously during growth, as part of a programmed event such as meiosis or as the result of exposure to environmental genotoxic agents. Multiple mechanisms exist to repair DSBs, including nonhomologous end joining and homologous recombination (HR) (Paques and Haber, 1999;Symington, 2002). The HR pathway serves to maintain all original genetic information during DSB repair. Many components of that pathway have been identified and characterized (Paques and Haber, 1999;Symington, 2002). HR involves multiple steps. The DSB is first resected to generate a recombinogenic 3Ј overhang that invades a homologous sequence (e.g., sister chromatid), forming a displacement or D-loop. The invasion step is catalyzed by a number of proteins including the Escherichia coli RecA homologue, Rad51. D-loop formation primes repair synthesis, which is followed by resolution of the recombined duplexes and ligation, producing intact duplex DNA molecules (Paques and Haber, 1999;Symington, 2002). The resolution of recombined DNA duplexes can yield products in which there has been reciprocal exchange of flanking markers (crossover) or not. During mitotic growth gene conversion is infrequently accompanied by crossover, whereas during meiosis, crossover recombination is much more prevalent (Paques and Haber, 1999).Efficient DNA repair requires modulation of both local and higher order chromatin structure. Interestingly, the structural maintenance of chromosomes (SMC) proteins have recently been recognized as important players in DNA repair (Hirano, 2002;Jessberger...

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Sister Chromatid Cohesion

2004

Encyclopedic Dictionary of Genetics, Genomics and Proteomics

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During S phase, not only does DNA have to be replicated, but also newly synthesized DNA molecules have to be connected with each other. This sister chromatid cohesion is essential for the biorientation of chromosomes on the mitotic or meiotic spindle, and is thus an essential prerequisite for chromosome segregation. Cohesion is mediated by cohesin complexes that are thought to embrace sister chromatids as large rings. Cohesin binds to DNA dynamically before DNA replication and is converted into a stably DNA-bound form during replication. This conversion requires acetylation of cohesin, which in vertebrates leads to recruitment of sororin. Sororin antagonizes Wapl, a protein that is able to release cohesin from DNA, presumably by opening the cohesin ring. Inhibition of Wapl by sororin therefore "locks" cohesin rings on DNA and allows them to maintain cohesion for long periods of time in mammalian oocytes, possibly for months or even years.

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Molecular Architecture of SMC Proteins and the Yeast Cohesin Complex

Cited by 669 publications

References 35 publications

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Nse1, Nse2, and a Novel Subunit of the Smc5-Smc6 Complex, Nse3, Play a Crucial Role in Meiosis

Sister Chromatid Cohesion

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