A DNA-BINDING PROTEIN CONTAINING 2 WIDELY SEPARATED ZINC FINGER MOTIFS THAT RECOGNIZE THE SAME DNA-SEQUENCE
A DNA-BINDING PROTEIN CONTAINING 2 WIDELY SEPARATED ZINC FINGER MOTIFS THAT RECOGNIZE THE SAME DNA-SEQUENCE
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DOI：
10.1101/gad.4.1.29
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发表时间：
1990-01-01
影响因子：
10.5
通讯作者：
MANIATIS, T
中科院分区：
文献类型：
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作者：
FAN, CM;MANIATIS, T
我们已经分离了编码特异性结合人IFN-β的正调控结构域（PRDII）的蛋白质（PRDII-BF 1）的全长cDNA克隆。基因启动子中的类似序列，以及存在于许多其它启动子和增强子中的类似序列。该蛋白的序列揭示了两个新的结构特征。首先，它是迄今为止报道的最大的序列特异性DNA结合蛋白（298 kD）。第二，它包含两组广泛分离的C2-H2型锌指。值得注意的是，每组锌指以相似的亲和力和甲基化干扰模式与相同的DNA序列基序结合。因此，这种蛋白质可以通过同时结合相同识别序列的重复拷贝来起作用。虽然PRDII-BF 1的功能尚不清楚，但其mRNA水平可由血清和病毒诱导，尽管动力学不同。
We have isolated a full-length cDNA clone encoding a protein (PRDII-BF1) that binds specifically to a positive regulatory domain (PRDII) of the human IFN-.beta. gene promoter, and to a similar sequence present in a number of other promoters and enhancers. The sequence of this protein reveals two novel structural features. First, it is the largest sequence-specific DNA-binding protein reported to date (298 kD). Second, it contains two widely separated sets of C2-H2-type zinc fingers. Remarkably, each set of zinc fingers binds to the same DNA sequence motif with similar affinities and methylation interference patterns. Thus, this protein may act by binding simulatneously to reiterated copies of the same recognition sequence. Although the function of PRDII-BF1 is not known, the level of its mRNA is inducible by serum and virus, albeit with different kinetics.