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Purified Smc5/6 complex exhibits DNA substrate recognition and compaction

ABSTRACT: Investigation into the topology and fucntion of the yeast SMC5/6 complex

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Francis O'Reilly

LAB HEAD: Juri Rappsilber

PROVIDER: PXD016196 | Pride | 2021-02-10

REPOSITORIES: Pride

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			Action	DRS
	B181202_02_Lumos_FO_CO_120_SMC56_BS3_SEC10_rep1.raw	Raw
	B181202_03_Lumos_FO_CO_120_SMC56_BS3_SEC9_rep1.raw	Raw
	B181202_04_Lumos_FO_CO_120_SMC56_BS3_SEC8_rep1.raw	Raw
	B181202_05_Lumos_FO_CO_120_SMC56_BS3_SEC7_rep1.raw	Raw
	B181202_06_Lumos_FO_CO_120_SMC56_BS3_SEC6_rep1.raw	Raw

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Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction.

Gutierrez-Escribano Pilar P Hormeño Silvia S Madariaga-Marcos Julene J Solé-Soler Roger R O'Reilly Francis J FJ Morris Kyle K Aicart-Ramos Clara C Aramayo Ricardo R Montoya Alex A Kramer Holger H Rappsilber Juri J Torres-Rosell Jordi J Moreno-Herrero Fernando F Aragon Luis L

Molecular cell 20201209 6

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 t ...[more]

PMID: 33301732

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