Schäfer U, Rausch O, Bouwmeester T, Pieler T
Otto-Warburg-Laboratorium, Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
Eur J Biochem. 1994 Dec 1;226(2):567-76. doi: 10.1111/j.1432-1033.1994.tb20082.x.
XFG 20-1 is one of several hundred C2H2-type zinc finger proteins of unknown biological function in Xenopus. Affinity selection of genomic DNA fragments identifies a 54-bp consensus sequence with high affinity for the XFG 20-1 protein. This sequence is part of a conserved inverted repeat in REM-1, a 0.5-kb repetitive, dispersed genomic DNA element. This finding indicates a possible link between the non-conserved nature of a large subgroup of DNA-binding C2H2 zinc finger proteins and the non-conserved nature of putative genomic target sequences. The 19 zinc finger modules of XFG 20-1 are organized in three structurally distinct groups. Of these, only the first and third ones are required and are sufficient for high-affinity DNA binding. The finding that removal of five internal zinc finger units does not alter the DNase I protection pattern of the complex formed is indicative of a high degree of structural flexibility for linear arrays of zinc fingers, which we imagine to adopt a more rigid structure only upon interaction with their nucleic acid partner molecules.
XFG 20-1是非洲爪蟾中数百种生物功能未知的C2H2型锌指蛋白之一。对基因组DNA片段进行亲和筛选,鉴定出一个与XFG 20-1蛋白具有高亲和力的54个碱基对的共有序列。该序列是REM-1中一个保守反向重复序列的一部分,REM-1是一个0.5 kb的重复性、分散性基因组DNA元件。这一发现表明,一大类DNA结合C2H2锌指蛋白的非保守性质与假定的基因组靶序列的非保守性质之间可能存在联系。XFG 20-1的19个锌指模块分为三个结构不同的组。其中,只有第一组和第三组是高亲和力DNA结合所必需且足够的。去除五个内部锌指单元不会改变所形成复合物的DNase I保护模式,这一发现表明锌指线性阵列具有高度的结构灵活性,我们认为锌指只有在与核酸伴侣分子相互作用时才会采用更刚性的结构。