Fig. 4: Dsup fractionates with yeast chromatin and associates across the yeast genome without apparent bias. | Nature Communications

Fig. 4: Dsup fractionates with yeast chromatin and associates across the yeast genome without apparent bias.

From: Multivalent binding of the tardigrade Dsup protein to chromatin promotes yeast survival and longevity upon exposure to oxidative damage

Fig. 4

a The Dsup HMGN-like motif (aa 363-370) and C-terminal region (aa 371-445) are required for the association with yeast chromatin. Yeast spheroblasts (Input) from indicated strains were resolved to Soluble and Chromatin fractions and immunoblotted as indicated. Confirming effective fractionation: GAPDH is a soluble protein, H2A is chromatin bound. EV, Empty vector. The samples detected for FLAG were resolved on one gel and the same samples were ran on a second gel to detect GAPDH and H2A. b CUT&RUN to examine Dsup allele interactions across the yeast genome (anti-FLAG). For each strain IgG (assay background) and anti-H3K4me3 (active gene promoters) were respectively included as negative and positive controls. Each target is group-scaled (after normalization to E.coli spike-in) to the highest signal in the depicted IGV window (IgG (82); H3K4me3 (1356) or Dsup-FLAG (311)). Data is from a representative CUT&RUN of biological replicates (sequence statistics in Supplementary Data File 2). Source data are provided as a Source Data file.

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