The cohesin ring uses its hinge to organize DNA using non-topological as well as topological mechanisms
| Autor: | Thomas G. Gligoris, Vincenzo Costanzo, Bin Hu, Maria Wissler, Sugako Ogushi, James E Collier, Kim Nasmyth, Johanna C. Scheinost, Alexander Kurze, Menelaos Voulgaris, Madhusudhan Srinivasan, Kok-Lung Chan, Naomi J Petela |
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| Rok vydání: | 2017 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Chromosomal Proteins Non-Histone Protein Conformation Mutant Hinge cohesin Cell Cycle Proteins Saccharomyces cerevisiae Chromatids Biology Topology Article Mice 03 medical and health sciences chemistry.chemical_compound Adenosine Triphosphate 0302 clinical medicine ATP hydrolysis Animals Humans 030304 developmental biology chromosome condensation 0303 health sciences loop extrusion Binding Sites Cohesin SMC condensin Hydrolysis Lysine Nuclear Proteins DNA Chromatin sister chromatid cohesion Establishment of sister chromatid cohesion chemistry Mutation biological phenomena cell phenomena and immunity 030217 neurology & neurosurgery |
| Zdroj: | Cell |
| ISSN: | 1097-4172 0092-8674 |
| DOI: | 10.1101/197848 |
| Popis: | Summary As predicted by the notion that sister chromatid cohesion is mediated by entrapment of sister DNAs inside cohesin rings, there is perfect correlation between co-entrapment of circular minichromosomes and sister chromatid cohesion. In most cells where cohesin loads without conferring cohesion, it does so by entrapment of individual DNAs. However, cohesin with a hinge domain whose positively charged lumen is neutralized loads and moves along chromatin despite failing to entrap DNAs. Thus, cohesin engages chromatin in non-topological, as well as topological, manners. Since hinge mutations, but not Smc-kleisin fusions, abolish entrapment, DNAs may enter cohesin rings through hinge opening. Mutation of three highly conserved lysine residues inside the Smc1 moiety of Smc1/3 hinges abolishes all loading without affecting cohesin’s recruitment to CEN loading sites or its ability to hydrolyze ATP. We suggest that loading and translocation are mediated by conformational changes in cohesin’s hinge driven by cycles of ATP hydrolysis. Graphical Abstract Highlights • Chromatid cohesion is mediated by co-entrapment of sister DNAs inside cohesin rings • Cohesin engages chromatin in non-topological as well as topological manners • Cohesin loads onto chromatin despite closure of any of the three ring interfaces. • Cohesin’s hinge domain is critical for non-topological and topological DNA association. Cohesin can selectively engage DNA without entrapping it, suggesting a new dimension to cohesin function. |
| Databáze: | OpenAIRE |
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