Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction

Eukaryotic SMC complexes, cohesin, condensin, and Smc5/6, use ATP hydrolysis to power a plethora of functions requiring organization and restructuring of eukaryotic chromosomes in interphase and during mitosis. The Smc5/6 mechanism of action and its activity on DNA are largely unknown. Here we purif...

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Vydáno v:Molecular cell Ročník 80; číslo 6; s. 1039
Hlavní autoři: Gutierrez-Escribano, Pilar, Hormeño, Silvia, Madariaga-Marcos, Julene, Solé-Soler, Roger, O'Reilly, Francis J, Morris, Kyle, Aicart-Ramos, Clara, Aramayo, Ricardo, Montoya, Alex, Kramer, Holger, Rappsilber, Juri, Torres-Rosell, Jordi, Moreno-Herrero, Fernando, Aragon, Luis
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 17.12.2020
Témata:
Adenosine Triphosphatases - genetics
Biophysical Phenomena
Cell Cycle Proteins - genetics
Cell Cycle Proteins - ultrastructure
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - ultrastructure
Cohesins
DNA-Binding Proteins - genetics
Humans
Interphase - genetics
Mitosis - genetics
Multiprotein Complexes - genetics
Multiprotein Complexes - ultrastructure
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - ultrastructure
Sumoylation - genetics
electron mmicroscopy
single-molecule
magnetic tweezers
Smc5/6 holocomplex
plectoneme stabilisation
Smc5/6 purification
DNA compaction
DNA substrate recognition
ISSN:1097-4164, 1097-4164
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Shrnutí:Eukaryotic SMC complexes, cohesin, condensin, and Smc5/6, use ATP hydrolysis to power a plethora of functions requiring organization and restructuring of eukaryotic chromosomes in interphase and during mitosis. The Smc5/6 mechanism of action and its activity on DNA are largely unknown. Here we purified the budding yeast Smc5/6 holocomplex and characterized its core biochemical and biophysical activities. Purified Smc5/6 exhibits DNA-dependent ATP hydrolysis and SUMO E3 ligase activity. We show that Smc5/6 binds DNA topologically with affinity for supercoiled and catenated DNA templates. Employing single-molecule assays to analyze the functional and dynamic characteristics of Smc5/6 bound to DNA, we show that Smc5/6 locks DNA plectonemes and can compact DNA in an ATP-dependent manner. These results demonstrate that the Smc5/6 complex recognizes DNA tertiary structures involving juxtaposed helices and might modulate DNA topology by plectoneme stabilization and local compaction.
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SourceType-Scholarly Journals-1
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content type line 23
ISSN:1097-4164
1097-4164
DOI:10.1016/j.molcel.2020.11.012