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. 2018 Feb 23;62(3):e01924-17. doi: 10.1128/AAC.01924-17

FIG 1.

FIG 1

ADA2 deletion results in decreased acetylation of H3K9 but not H3K14. (A) C. glabrata strains were cultured, and the total proteins were extracted to determine the acetylation level of histone 3 via Western blotting. A total of 15 μg of protein was probed with anti-H3K9ac antibody and 45 μg was probed with anti-H3K14ac antibody. Actin was used as a loading control in all blots. (B) Acetylation levels of H3K9 and H3K14 in the C. glabrata wild type (WT), the ada2 mutants, and the complemented strain were determined from three independent Western blot experiments. The blots were analyzed using ImageJ software, and the signals were normalized to the actin signals. The results are represented as the mean ± standard deviation. Asterisks indicate statistically significant differences compared with the results for the wild type using an unpaired t test (**, P < 0.01; ***, P < 0.0001).