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. 2009 Dec 1;20(23):4976–4984. doi: 10.1091/mbc.E09-04-0295

Figure 1.

Figure 1.

Heat shock induces a deacetylation of core histones. (A) Heat shock induces a decrease in nuclear acetylation level. Acetylated proteins were detected by immunofluorescence with an anti-acetylated lysine antibody in HeLa cells exposed (+) or not (−) to a 1-h heat shock at 43°C. Nuclei were counterstained with DAPI. Acetylated nuclear foci corresponding to the nuclear stress bodies are present in heat-shocked cells. Bar, 5 μm. (B) Heat shock induces a reversible deacetylation of H4. Whole cell extracts from HeLa exposed to different conditions of heat shock were analyzed by Western blot using an anti-acetylated H4 antibody: 37°C (−), heat shock 1 h at 43°C (0), 3 h (3), or 5 h (5) of recovery after the 1-h heat shock. H2B was used as loading control. (C) Heat shock does not affect histone level and solubility. Cytosolic (C), nuclear soluble (NS), and nuclear insoluble (NI) protein extracts from cells exposed (+) or not (−) to a 1-h heat shock at 43°C or recovery were run on 15% acrylamide and stained with Coomassie blue, and the same fractions were analyzed by Western blot with an anti-H2B antibody.