Volume 16, No 6, Jun 2006
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 16 Issue 6, June 2006: 566-576
ORIGINAL ARTICLES
Effects of histone deacetylase inhibitors on transcriptional regulation of the hsp70 gene in Drosophila
Yan Mei Zhao, Xia Chen, Hui Sun, Zhi Gen Yuan, Guo Ling Ren, Xiao Xue Li,Jun Lu, Bai Qu Huang
1The Institute of Genetics and Cytology, Northeast Normal University, Changchun 130024, China
Correspondence: Jun Lu(ycsuo@nenu.edu.cn, luj809@nenu.edu.cn)
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.
Cell Research (2006) 16:566-576. doi:10.1038/sj.cr.7310074; published online 15 June 2006
FULL TEXT | PDF
Browse 1787
