ISOLATION OF A RECOMBINANT COPY OF THE GENE ENCODING C/EBP
ISOLATION OF A RECOMBINANT COPY OF THE GENE ENCODING C/EBP
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DOI：
10.1101/gad.2.7.786
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发表时间：
1988-07-01
影响因子：
10.5
通讯作者：
MCKNIGHT, SL
中科院分区：
文献类型：
--
作者：
LANDSCHULZ, WH;JOHNSON, PF;MCKNIGHT, SL
在先前的两项研究中，我们描述了大鼠肝细胞核中存在的热稳定DNA结合蛋白的性质。该蛋白质，下文称为C/EBP，能够选择性结合几种病毒启动子的CCAAT同源性（Graves等，1986），以及许多病毒增强子共有的核心同源性（约翰逊等，1987年）。我们现在报道编码C/EBP的基因的重组克隆的分离。克隆在细菌细胞中的表达产生了一种蛋白质，该蛋白质在体外与CCAAT同源性和增强子核心同源性结合，提供了单一基因产物导致两种结合活性的确凿证据。通过研究C/EBP蛋白酶衍生片段的性质，我们将其DNA结合结构域定位于14 kD片段。位于C/EBP的DNA结合结构域内的60个氨基酸片段与myc和fos癌基因的产物具有序列相似性。
In two previous studies we described the properties of a heat-stable DNA-binding protein present in rat liver nuclei. This protein, hereafter termed C/EBP, is capable of selective binding to the CCAAT homology of several viral promoters (Graves et al. 1986), as well as the core homology common to many viral enhancers (Johnson et at. 1987). we now report the isolation of a recombinant clone of the gene that encodes C/EBP. Expression of the clone in bacterial cells yields a protein that binds in vitro to both the CCAAT homology and the enhancer core homology, providing conclusive evidence that a single gene product accounts for both binding activities. By examining the properties of protease-derived fragments of C/EBP, we have localized its DNA-binding domain to a 14-kD fragment. A 60-amino-acid segment located within the DNA-binding domain of C/EBP bears sequence similarity to the products of the myc and fos oncogenes.