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首页> 外文期刊>Molecular and Cellular Biology >Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).
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Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

机译：纯化和鉴定59千达尔顿蛋白质，该蛋白质与石棺（Sarcophaga peregrina）（果蝇）的防御蛋白基因的NF-κB结合基序特异性结合。

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摘要

Various Sarcophaga peregrina (flesh fly) defense protein genes were shown to be activated when NIH-Sape-4 cells were cultured with bacterial lipopolysaccharides or beta-1,3-glucan. The 5' upstream regions of the defense protein genes were found to have common motifs showing similarity to the mammalian NF-kappa B-binding consensus sequence. A protein with affinity to the NF-kappa B-binding motif of the Sarcophaga lectin promoter was identified and purified to near homogeneity. This 59-kDa protein also bound to the NF-kappa B-binding motifs of other defense protein genes, e.g., sarcotoxin I and sarcotoxin II genes. This protein was found in both the cytoplasmic and the nuclear fractions of the cells, and it appeared to migrate from the cytoplasm to the nucleus on treatment of the cells with lipopolysaccharides. This 59-kDa protein is probably a transcriptional regulator of the genes for defense proteins of S. peregrina.
机译：当NIH-Sape-4细胞与细菌脂多糖或β-1,3-葡聚糖一起培养时，各种Sarcophaga peregrina（果蝇）防御蛋白基因被激活。发现防御蛋白基因的5'上游区域具有显示与哺乳动物NF-κB结合共有序列相似的共同基序。鉴定出对石棺凝集素启动子的NF-κB结合基序具有亲和力的蛋白质，并纯化至接近均一。该59-kDa蛋白还与其他防御蛋白基因例如肌毒素I和肌毒素II基因的NF-κB结合基序结合。在细胞的细胞质和细胞核级分中都发现了这种蛋白质，并且在用脂多糖处理细胞时，它似乎从细胞质迁移到细胞核。该59 kDa蛋白可能是S. peregrina防御蛋白基因的转录调节因子。

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