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    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 activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex. © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.


    Stephen T Hallett, Pascale Schellenberger, Lihong Zhou, Fabienne Beuron, Ed Morris, Johanne M Murray, Antony W Oliver. Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex. Nucleic acids research. 2021 May 07;49(8):4534-4549

    PMID: 33849072

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