{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hallett ST"],"funding":["Medical Research Council"],"pagination":["4534-4549"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8096239"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["49(8)"],"pubmed_abstract":["The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase"],"journal":["Nucleic acids research"],"pubmed_title":["Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex."],"pmcid":["PMC8096239"],"funding_grant_id":["MR/P018955/1","G1001668"],"pubmed_authors":["Schellenberger P","Zhou L","Beuron F","Hallett ST","Oliver AW","Morris E","Murray JM"],"additional_accession":[]},"is_claimable":false,"name":"Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex.","description":"The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2026-04-18T01:38:06.069Z","creation":"2022-02-10T18:53:15.029Z"},"accession":"S-EPMC8096239","cross_references":{"pubmed":["33849072"],"doi":["10.1093/nar/gkab234"]}}