Abstract
Histone acetyltransferases/deacetylases contribute to the activation or inactivation of transcription by modifying the structure of chromatin. Here we examined the effects of histone deacetylase inhibitors (HDIs), trichostatin A, and sodium butyrate on hsp70 gene transcriptional regulation in Drosophila. The chromatin immunoprecipitation assays revealed that HDI treatments induced the hyperacetylation of histone H3 at the promoter and the transcribing regions of hsp70 gene, increased the accessibility of heat-shock factor to target heat-shock element, and promoted the RNA polymerase II-mediated transcription. Moreover, the quantitative real-time PCR confirmed that the HDI-induced hyperacetylation of histone H3 enhanced both the basal and the inducible expression of hsp70 mRNA level. In addition, the acetylation level of histone H3 at the promoter exhibited a fluctuated change upon the time of heat shock. These experimental data implicated a causal link between histone acetylation and enhanced transcription initiation of hsp70 gene in Drosophila.
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Abbreviations
- HDI:
-
histone deacetylase inhibitor
- Hsp:
-
heat shock protein
- TSA:
-
trichostatin A
- BuA:
-
sodium butyrate
- HAT:
-
histone acetyltransferase
- HDAC:
-
histone deacetylase
- ChIP:
-
chromatin immunoprecipitation
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Acknowledgements
We thank Prof C Wu (Laboratory of Biochemistry, NCI, NIH) and JT Lis (Department of Molecular Biology and Genetics, College of Agriculture and life Sciences, Cornell University) for providing antibodies. This work was supported by grants from The National Basic Research Program of China (2005CB522404) and The National Nature Science Foundation of China (30571698).
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Zhao, Y., Chen, X., Sun, H. et al. Effects of histone deacetylase inhibitors on transcriptional regulation of the hsp70 gene in Drosophila. Cell Res 16, 566–576 (2006). https://doi.org/10.1038/sj.cr.7310074
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DOI: https://doi.org/10.1038/sj.cr.7310074
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