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一种含有两个相距甚远的锌指基序的DNA结合蛋白,这两个基序识别相同的DNA序列。

A DNA-binding protein containing two widely separated zinc finger motifs that recognize the same DNA sequence.

作者信息

Fan C M, Maniatis T

机构信息

Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

出版信息

Genes Dev. 1990 Jan;4(1):29-42. doi: 10.1101/gad.4.1.29.

Abstract

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 simultaneously 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.

摘要

我们分离出了一个全长cDNA克隆,它编码一种蛋白质(PRDII-BF1),该蛋白质能特异性地结合人干扰素-β基因启动子的一个正调控结构域(PRDII),以及许多其他启动子和增强子中存在的类似序列。这种蛋白质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)。其次,它包含两组相距很远的C2-H2型锌指。值得注意的是,每组锌指都以相似的亲和力和甲基化干扰模式结合相同的DNA序列基序。因此,这种蛋白质可能通过同时结合相同识别序列的重复拷贝来发挥作用。虽然PRDII-BF1的功能尚不清楚,但其mRNA水平可被血清和病毒诱导,尽管动力学不同。

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