Malin Stephen, Linderson Ylva, Almqvist Jenny, Ernberg Ingemar, Tallone Tiziano, Pettersson Sven
Department of Microbiology and Tumor biology Box 280, Karolinska Institutet, 171 77 Stockholm, Sweden.
Nucleic Acids Res. 2005 Aug 15;33(14):4618-25. doi: 10.1093/nar/gki744. Print 2005.
POU domain proteins contain a bipartite DNA-binding element that can confer allosteric control of coactivator recruitment. Dimerization of Oct-1 and Oct-2 on palindromic response elements results in the conformational dependent inclusion or exclusion of the transcriptional coactivator OBF-1. In this paper, we demonstrate that Oct-1 and Oct-2 can function as transcriptional repressors by recruiting and physically interacting with members of the Grg/TLE family of corepressors. In accordance with a model of DNA induced cofactor assembly, and analogous to the recruitment of the OBF-1 coactivator, the different Grg/TLE members can discriminate between both Oct-1 and Oct-2, and the monomeric or dimeric nature of the POU/DNA complex.
POU结构域蛋白包含一个双组分DNA结合元件，该元件可对共激活因子的募集进行变构控制。Oct-1和Oct-2在回文反应元件上的二聚化导致转录共激活因子OBF-1根据构象依赖性被包含或排除。在本文中，我们证明Oct-1和Oct-2可通过与共抑制因子Grg/TLE家族成员募集并发生物理相互作用而发挥转录抑制因子的作用。根据DNA诱导的辅因子组装模型，并且类似于OBF-1共激活因子的募集，不同的Grg/TLE成员可以区分Oct-1和Oct-2以及POU/DNA复合物的单体或二聚体性质。
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