Journal: Nature Communications
Article Title: Reprogramming of bacterial virulence by lysine acetylation
doi: 10.1038/s41467-026-72244-8
Figure Lengend Snippet: a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the absorption at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
Article Snippet: Elution fractions containing pure protein were pooled and concentrated before protein concentration was determined by measuring absorption at 280 nm using a spectrophotometer DS-11 FX (DeNovix, Wilmington USA).
Techniques: Western Blot, Staining, Control, SDS Page
