Fig. 1: Sir2 alone in SaSir2-HerA does not exhibit NADase activity, which can be activated upon the binding of HerA. | Nature Communications

Fig. 1: Sir2 alone in SaSir2-HerA does not exhibit NADase activity, which can be activated upon the binding of HerA.

From: Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system

Fig. 1

a Schematic diagram of the Sir2 and HerA operon of S. aureus. b In vitro NADase activity of SaSir2 and SaSir2-HerA; SaSir2 could not hydrolyze NAD+; in contrast, a mixture of SaSir2 and SaHerA exhibited NADase activity. c The gel filtration profile and SDS‒PAGE results of copurified SaSir2-HerA. d AUC result for apo SaSir2, suggesting that it behaved as a homodimer in solution. e Effects of different concentrations of ATP on the NADase activity of SaSir2-HerA. Data were presented as mean ± SD in histograms; n = 3 independent experiments. P-value determined by paired two-tailed t-tests is indicated in the figure. Source data are provided as a Source Data file.

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