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)
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)
复制标题
59 千道尔顿蛋白质的纯化和表征,该蛋白质与 Sarcophaga peregrina(肉蝇)防御蛋白基因的 NF-kappa B 结合基序特异性结合
DOI:
10.1128/mcb.13.7.4049-4056.1993
复制
发表时间:
1993
影响因子:
5.3
通讯作者:
Shunji Natori
中科院分区:
文献类型:
--
作者:
Ayako Kobayashi;Mayumi Matsui;T. Kubo;Shunji Natori
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.
DOI:
10.1073/pnas.85.13.4700
发表时间:
1988
影响因子:
11.1
作者:
Kawakami,K;Scheidereit,C;Roeder,RG
通讯作者:
Roeder,RG