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热休克蛋白70i(hsp70i)基因标记机制。

Mechanism of hsp70i gene bookmarking.

作者信息

Xing Hongyan, Wilkerson Donald C, Mayhew Christopher N, Lubert Eric J, Skaggs Hollie S, Goodson Michael L, Hong Yiling, Park-Sarge Ok-Kyong, Sarge Kevin D

机构信息

Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536, USA.

出版信息

Science. 2005 Jan 21;307(5708):421-3. doi: 10.1126/science.1106478.

Abstract

In contrast to most genomic DNA in mitotic cells, the promoter regions of some genes, such as the stress-inducible hsp70i gene that codes for a heat shock protein, remain uncompacted, a phenomenon called bookmarking. Here we show that hsp70i bookmarking is mediated by a transcription factor called HSF2, which binds this promoter in mitotic cells, recruits protein phosphatase 2A, and interacts with the CAP-G subunit of the condensin enzyme to promote efficient dephosphorylation and inactivation of condensin complexes in the vicinity, thereby preventing compaction at this site. Blocking HSF2-mediated bookmarking by HSF2 RNA interference decreases hsp70i induction and survival of stressed cells in the G1 phase, which demonstrates the biological importance of gene bookmarking.

摘要

与有丝分裂细胞中的大多数基因组DNA不同,某些基因的启动子区域,如编码热休克蛋白的应激诱导型hsp70i基因,仍未压缩,这种现象称为书签化。我们在此表明,hsp70i书签化由一种名为HSF2的转录因子介导,该因子在有丝分裂细胞中结合此启动子,招募蛋白磷酸酶2A,并与凝聚素酶的CAP-G亚基相互作用,以促进附近凝聚素复合物的有效去磷酸化和失活,从而防止该位点的压缩。通过HSF2 RNA干扰阻断HSF2介导书签化会降低hsp70i诱导以及G1期应激细胞的存活率,这证明了基因书签化的生物学重要性。

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