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 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.
Mesh Terms:
Adenosine Triphosphatases, Biophysical Phenomena, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Humans, Interphase, Mitosis, Multiprotein Complexes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sumoylation
Mol Cell
Date: Dec. 17, 2019
Download Curated Data For This Publication
226828
Switch View:
  • Interactions 220