Bandyopadhyay S K, Kalvakolanu D V, Sen G C
Department of Molecular Biology, Cleveland Clinic Foundation, Ohio 44195-5069.
Mol Cell Biol. 1990 Oct;10(10):5055-63. doi: 10.1128/mcb.10.10.5055-5063.1990.
HeLaM is a variant cell line in which the transcriptional induction of many genes by alpha interferon has special characteristics (Tiwari et al., Mol. Cell. Biol. 8:4289-4294, 1988). The same characteristics were also displayed for induced transcription of a permanently transfected chimeric gene containing the interferon-stimulated response element of gene 561. For understanding the molecular basis of the special requirements of HeLaM cells, an analysis of the interferon-stimulated gene factors (ISGF) was undertaken. By using gel shift assays, it was shown that the activation of ISGF3 by alpha interferon treatment of HeLaM cells had characteristics identical to those of induced transcription: inhibition by 2-aminopurine and the need for ongoing protein synthesis which was obviated by pretreating the cells with gamma interferon. Upon mixing in vitro the cytoplasmic fraction of gamma interferon-treated HeLaM cells with that of cells treated with alpha interferon and cycloheximide, active ISGF3 was reconstituted, presumably through complementation of two components, ISGF3 gamma and ISGF3 alpha, present in the two respective fractions. Because, unlike other cells, untreated HeLaM cells did not contain detectable levels of either component, we could induce them individually and study their independent properties. Induction of ISGF3 gamma but not of ISGF3 alpha needed ongoing protein synthesis and was blocked by 2-aminopurine. Once induced, ISGF3 gamma was active for 24 h and was present in both the nuclear and cytoplasmic fractions. Activated ISGF3 alpha, on the other hand, did not translocate to the nucleus in the absence of ISGF3 gamma, and in the cytoplasm its activity decayed within 2 h of its activation. In reference to our working model, all of the above observations indicate that ISGF3 gamma is the product of signal 1 and ISGF3 alpha is the product of signal 2.
HeLaM是一种变异细胞系,其中α干扰素对许多基因的转录诱导具有特殊特性(蒂瓦里等人,《分子与细胞生物学》8:4289 - 4294,1988年)。对于含有基因561的干扰素刺激反应元件的永久转染嵌合基因的诱导转录,也表现出同样的特性。为了理解HeLaM细胞特殊需求的分子基础,对干扰素刺激基因因子(ISGF)进行了分析。通过凝胶迁移分析表明,用α干扰素处理HeLaM细胞激活ISGF3具有与诱导转录相同的特性:被2 - 氨基嘌呤抑制,并且需要持续的蛋白质合成,而用γ干扰素预处理细胞可消除这种需求。将γ干扰素处理的HeLaM细胞的细胞质部分与用α干扰素和环己酰亚胺处理的细胞的细胞质部分在体外混合后,活性ISGF3得以重建,推测是通过两个相应部分中存在的两种成分ISGF3γ和ISGF3α的互补作用。因为与其他细胞不同,未处理的HeLaM细胞中两种成分的可检测水平均不存在,所以我们可以分别诱导它们并研究其独立特性。ISGF3γ的诱导而非ISGF3α的诱导需要持续的蛋白质合成,并被2 - 氨基嘌呤阻断。一旦被诱导,ISGF3γ在24小时内保持活性,并且存在于细胞核和细胞质部分。另一方面,在没有ISGF3γ的情况下,激活的ISGF3α不会转运到细胞核,并且在细胞质中其活性在激活后2小时内衰减。参照我们的工作模型,上述所有观察结果表明,ISGF3γ是信号1的产物,ISGF3α是信号2的产物。