Cohesin association to replication sites depends on Rad50 and promotes fork restart Journal Article
| Authors: | Tittel-Elmer, M.; Lengronne, A.; Davidson, M. B.; Bacal, J.; François, P.; Hohl, M.; Petrini, J. H. J.; Pasero, P.; Cobb, J. A. |
| Article Title: | Cohesin association to replication sites depends on Rad50 and promotes fork restart |
| Abstract: | The cohesin complex holds together newly replicated chromatids and is involved in diverse pathways that preserve genome integrity. We show that in budding yeast, cohesin is transiently recruited to active replication origins, and it spreads along DNA as forks progress. When DNA synthesis is impeded, cohesin accumulates at replication sites and is critical for the recovery of stalled forks. Cohesin enrichment at replication forks does not depend on γH2A(X) formation, which differs from its loading requirements at DNA double-strand breaks (DSBs). However, cohesin localization is largely reduced in rad50Δ mutants and in cells lacking both Mec1 and Tel1 checkpoint kinases. Interestingly, cohesin loading at replication sites depends on the structural features of Rad50 that are important for bridging sister chromatids, including the CXXC hook domain and the length of the coiled-coil extensions. Together, these data reveal a function for cohesin in the maintenance of genome integrity during S phase. © 2012 Elsevier Inc. |
| Keywords: | mutation; dna-binding proteins; hydroxyurea; dna replication; dna synthesis; protein localization; cohesin; cell cycle proteins; chromosomal proteins, non-histone; rad50 protein; cell cycle s phase; dna repair; sister chromatid; stress, physiological; chromatid; saccharomyces cerevisiae; protein-serine-threonine kinases; intracellular signaling peptides and proteins; dna breaks, double-stranded; double stranded dna break; saccharomyces cerevisiae proteins; saccharomycetales; histones; s phase; genes, fungal |
| Journal Title: | Molecular Cell |
| Volume: | 48 |
| Issue: | 1 |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press |
| Date Published: | 2012-10-12 |
| Start Page: | 98 |
| End Page: | 108 |
| Language: | English |
| DOI: | 10.1016/j.molcel.2012.07.004 |
| PROVIDER: | scopus |
| PUBMED: | 22885006 |
| PMCID: | PMC3904740 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 2 November 2012" - "CODEN: MOCEF" - "Source: Scopus" |
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