Luo Y, Amin J, Voellmy R
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.
Mol Cell Biol. 1991 Jul;11(7):3660-75. doi: 10.1128/mcb.11.7.3660-3675.1991.
Purification of ecdysterone receptor from Drosophila melanogaster to apparent homogeneity is reported. Purified receptor binds specifically to several sequences in the promoters of the developmentally active hsp27 and hsp23 heat shock genes that were previously implied in ecdysterone regulation of the genes and that share limited homology among themselves and with mammalian steroid receptor binding sites. Some of these elements confer ecdysterone regulation on a basal promoter in transfected cells, acting in a synergistic fashion. Transcription in vitro of promoters containing such elements is stimulated up to 100-fold by added purified ecdysterone receptor, depending on receptor dosage and the number of elements present. Transcriptional enhancement requires sequence-specific binding of receptor to template promoters which facilitates the formation of a preinitiation complex. Ecdysterone stimulates DNA binding of the receptor in vitro.
据报道,已从黑腹果蝇中纯化出了具有明显同质性的蜕皮激素受体。纯化后的受体可特异性结合发育活跃的hsp27和hsp23热休克基因启动子中的多个序列,这些序列先前被认为与蜕皮激素对这些基因的调控有关,它们彼此之间以及与哺乳动物类固醇受体结合位点具有有限的同源性。其中一些元件以协同方式在转染细胞中赋予基础启动子蜕皮激素调控作用。根据受体剂量和存在的元件数量,添加纯化的蜕皮激素受体可使含有此类元件的启动子的体外转录提高至100倍。转录增强需要受体与模板启动子进行序列特异性结合,这有助于形成预起始复合物。蜕皮激素在体外刺激受体与DNA的结合。