Holding Your Own: Establishing Sister Chromatid Cohesion

Skibbens, Robert V.

doi:10.1101/gr.153600

Cited by 43 publications

(43 citation statements)

References 86 publications

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“…Consistent with these dual activities, Mps1p is located at both the spindle pole and kinetochores. Similar kinetochore/spindle pole body co-localization has been reported for Mad2p, anaphase-promoting complex subunits, and a host of centromere-binding proteins (8,48). In parallel, numerous nuclear pore proteins now appear to associate with kinetochores in both yeast and mammalian cells and function in transcriptional repression (49 -51).…”

Section: Discussionsupporting

confidence: 72%

“…Recent findings that DNA helicases are required for sister chromatid cohesion (16,19,20) suggest that DNA helicases first encounter and possibly unwind DNA loci marked by cohesins. This model is supported by numerous observations that at least a subset of cohesins are associated with DNA after anaphase onset and prior to S-phase (21)(22)(23), suggesting that a cohesin subset remains from the previous cell cycle to mark loci destined for cohesion assembly reactions in the subsequent cell cycle (8,16). Intriguingly, DNA helicases, such as budding yeast Chl1p and Sgs1p, are homologs of human factors (BACH1, Blooms, and Werners) implicated in genome maintenance, aging, and cancer progression (16, 24 -27).…”

supporting

confidence: 55%

“…Several DNA replication factors now have been identified as functioning in cohesion, including replication factor C subunits, DNA helicases, and DNA polymerases (9 -16). These findings have popularized a model in which cohesion is established as nascent sister chromatids emerge from behind the DNA replication fork (8,17,18). Recent findings that DNA helicases are required for sister chromatid cohesion (16,19,20) suggest that DNA helicases first encounter and possibly unwind DNA loci marked by cohesins.…”

mentioning

confidence: 99%

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The Spindle Pole Body Assembly Component Mps3p/Nep98p Functions in Sister Chromatid Cohesion

Antoniacci

Kenna

Uetz

et al. 2004

Journal of Biological Chemistry

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For successful chromosome segregation during mitosis, several processes must occur early in the cell cycle, including spindle pole duplication, DNA replication, and the establishment of cohesion between nascent sister chromatids. Spindle pole body duplication begins in G 1 and continues during early S-phase as spindle pole bodies mature and start to separate. Key steps in spindle pole body duplication are the sequential recruitment of Cdc31p and Spc42p by the nuclear envelope transmembrane protein Msp3p/Nep98p (herein termed Mps3p). Concurrent with DNA replication, Ctf7p/Eco1p (herein termed Ctf7p) ensures that nascent sister chromatids are paired together, identifying the products of replication as sister chromatids. Here, we provide the first evidence that the nuclear envelope spindle pole body assembly component Mps3p performs a function critical to sister chromatid cohesion. Mps3p was identified as interacting with Ctf7p from a genome-wide two-hybrid screen, and the physical interaction was confirmed by both in vivo (co-immunoprecipitation) and in vitro (GST pull-down) assays. An in vivo cohesion assay on new mps3/nep98 alleles revealed that loss of Mps3p results in precocious sister chromatid separation and that Mps3p functions after G 1 , coincident with Ctf7p. Mps3p is not required for cohesion during mitosis, revealing that Mps3p functions in cohesion establishment and not maintenance. Mutated Mps3p that results in cohesion defects no longer binds to Ctf7p in vitro, demonstrating that the interaction between Mps3p and Ctf7p is physiologically relevant. In support of this model, mps3 ctf7 double mutant cells exhibit conditional synthetic lethality. These findings document a new role for Mps3p in sister chromatid cohesion and provide novel insights into the mechanism by which a spindle pole body component, when mutated, contributes to aneuploidy.Microtubule-organizing center duplication, separation, and microtubule nucleation are all essential facets of proper chromosome segregation. In budding yeast, microtubule-organizing centers, called spindle pole bodies, function on both sides of the nuclear envelope to nucleate microtubules in both the cytoplasmic and nuclear volumes. Spindle pole body duplication is a multistep process that includes formation of a satellite, expansion into a cytoplasmic duplication plaque, half-bridge growth, and subsequent insertion into the nuclear envelope (1, 2). Evidence from genetic and electron microscopy studies indicates that spindle pole body duplication starts in G 1 and continues into early S-phase. Mps3p/Nep98p (herein termed Mps3p) is an essential nuclear envelope protein that is concentrated at the nuclear envelope half-bridge and required for spindle pole body assembly. Early in spindle pole body assembly, Mps3p functions to recruit and anchor Cdc31p to the half-bridge. Later, Mps3p is required for integration of Spc42p into the spindle pole duplication plaque (3, 4).Coincident with the latter portion of spindle pole body maturation and separation are the processes ...

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Section: Discussionsupporting

confidence: 72%

supporting

confidence: 55%

mentioning

confidence: 99%

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The Spindle Pole Body Assembly Component Mps3p/Nep98p Functions in Sister Chromatid Cohesion

Antoniacci

Kenna

Uetz

et al. 2004

Journal of Biological Chemistry

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“…In this Commentary, we propose a model in which cohesion depends on multiple mechanisms that collaborate to ensure cohesion along the length of the whole chromosome. Koshland and Guacci, 2000;Nasmyth and Schleiffer, 2004;Skibbens, 2000). Only telomeres lose cohesion in 100% of cohesin-mutant cells, whereas loci at the chromosome arms and pericentromere remain cohered in 40-75% of cells and the ribosomal DNA (rDNA) locus remains cohered in the majority of cohesin-mutant cells (Fig.…”

Section: Introductionmentioning

confidence: 99%

Chromosome cohesion – rings, knots, orcs and fellowship

Díaz-Martínez

Giménez-Abián²,

Clarke

2008

Journal of Cell Science

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Sister-chromatid cohesion is essential for accurate chromosome segregation. A key discovery towards our understanding of sister-chromatid cohesion was made 10 years ago with the identification of cohesins. Since then, cohesins have been shown to be involved in cohesion in numerous organisms, from yeast to mammals. Studies of the composition, regulation and structure of the cohesin complex led to a model in which cohesin loading during S-phase establishes cohesion, and cohesin cleavage at the onset of anaphase allows sister-chromatid separation. However, recent studies have revealed activities that provide cohesion in the absence of cohesin. Here we review these advances and propose an integrative model in which chromatid cohesion is a result of the combined activities of multiple cohesion mechanisms.

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“…4,7,8 Efficient establishment of cohesion requires proteins that facilitate cohesin complex localization to chromosomes prior to DNA replication (e.g., Scc2p), and that couple cohesion establishment with DNA replication (e.g., Ctf7p/Eco1p). 9 Pds5p is another chromosomal protein important for sister chromatid cohesion. [10][11][12][13][14] Pds5p and the cohesin complex colocalize on chromosomes at discrete loci.…”

Section: Introductionmentioning

confidence: 99%