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首页> 外文期刊>Molecular and Cellular Biology >Suppression of grp78 core promoter element-mediated stress induction by the dbpA and dbpB (YB-1) cold shock domain proteins.
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Suppression of grp78 core promoter element-mediated stress induction by the dbpA and dbpB (YB-1) cold shock domain proteins.

机译：抑制dbpA和dbpB（YB-1）冷休克域蛋白对grp78核心启动子元件介导的应激诱导。

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The highly conserved grp78 core promoter element plays an important role in the induction of grp78 under diverse stress signals. Previous studies have established a functional region in the 3' half of the core (stress-inducible change region [SICR]) which exhibits stress-inducible changes in stressed nuclei. The human transcription factor YY1 is shown to bind the SICR and transactivate the core element under stress conditions. Here we report that expression library screening with the core element has identified two new core binding proteins, YB-1 and dbpA. Both proteins belong to the Y-box family of proteins characterized by an evolutionarily conserved DNA binding motif, the cold shock domain (CSD). In contrast to YY1, which binds only double-stranded SICR, the Y-box/CSD proteins much prefer the lower strand of the SICR. The Y-box proteins can repress the inducibility of the grp78 core element mediated by treatment of cells with A23187, thapsigargin, and tunicamycin. In gel shift assays, YY1 binding to the core element is inhibited by either YB-1 or dbpA. A yeast interaction trap screen using LexA-YY1 as a bait and a HeLa cell cDNA-acid patch fusion library identified YB-1 as a YY1-interacting protein. In cotransfection experiments, the Y-box proteins antagonize the YY1-mediated enhancement of transcription directed by the grp78 core in stressed cells. Thus, the CSD proteins may be part of the stress signal transduction mechanism in the mammalian system.
机译：高度保守的grp78核心启动子元件在多种胁迫信号下的grp78诱导中起重要作用。先前的研究已经在核心的3'半部分建立了一个功能区域（应力诱导变化区域[SICR]），该区域在应力核中表现出应力诱导变化。显示人类转录因子YY1在压力条件下结合SICR并激活核心元件。在这里，我们报告表达库筛选与核心元素已经确定了两个新的核心结合蛋白，YB-1和dbpA。这两种蛋白质均属于Y-box蛋白质家族，其特征是进化上保守的DNA结合基序，即冷休克结构域（CSD）。与仅结合双链SICR的YY1相比，Y-box / CSD蛋白更喜欢SICR的较低链。 Y-box蛋白可以抑制通过用A23187，毒胡萝卜素和衣霉素处理细胞介导的grp78核心元件的诱导性。在凝胶位移测定中，YB-1或dbpA抑制YY1与核心元件的结合。酵母相互作用陷阱筛选使用LexA-YY1作为诱饵和HeLa细胞cDNA-酸补丁融合文库，鉴定YB-1为YY1相互作用蛋白。在共转染实验中，Y-box蛋白拮抗了在应激细胞中由grp78核心指导的YY1介导的转录增强。因此，CSD蛋白可能是哺乳动物系统中压力信号转导机制的一部分。

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