SOLUTION STRUCTURE OF MOUSE SRY DNA COMPLEX

锌结合基序在基因调控因子中普遍存在， 提供了金属依赖性蛋白质折叠的经济机制。 在早期的研究中，我们描述了一种新的锌结合基序， 人转录延伸因子核酸结合域 TFIIS。 NMR结构由三链反平行的 ?-这张纸指定的锌带。 序列数据库分析 提出了一个保守的家庭锌带图案在一个不同的家庭 包括RNA聚合酶本身。 一个假定的锌带序列的有趣发现， 古细菌基因组（Kaine，B. P.，梅尔，I. J.，& Woese，C.R.（1994）Proc. Natl. Acad. Sci. USA 91，3854-8）现在允许这个假设是 在异常热稳定性的系统中测试定向。 的 archeal基因编码与人类RNA亚基同源的蛋白质 聚合酶II。 我们建议，以确定解决方案的结构， RNA聚合酶亚基的多维异谱NMR方法。

Zn-binding motifs, ubiquitous among gene-regulatory factors, provide an economical mechanism of metal-dependent protein folding. In earlier studies we described a novel Zn-binding motif in the nucleic-acid binding domain of human transcriptional elongation factor TFIIS. The NMR structure consists of a three-stranded antiparallel ?-sheet designated the Zn ribbon. Analysis of the sequence database suggested a conserved family of Zn-ribbon motifs in a diverse family of nucleic-acid-binding proteins, including RNA polymerase itself. The intriguing discovery of a putative Zn ribbon sequence in an archeal genome (Kaine, B.P., Mehr, I.J., & Woese, C.R. (1994) Proc. Natl. Acad. Sci. USA 91, 3854-8) now permits this hypothesis to be tested directed in a system of exception thermal stability. The archeal gene encodes a protein homologous to a subunit of human RNA polymerase II. We propose to determine the solution structure of this RNA polymerase subunit by multidimensional heteronuclear NMR methods.