STRUCTURAL STUDIES OF COM, A VIRAL ZINC-FINGER PROTEIN

蛋白质控制核酸的转录和翻译是基本的 但识别的详细化学机制 绑定和控制的理解很少。 一系列的实验是 描述为研究翻译激活蛋白的结构， COM，从噬菌体Mu克隆，并研究其与 其同源核酸。 COM提供了一个简单的范例， proteins. 它是一个小的（62个氨基酸），单结构域，锌指 蛋白 具体的结构研究提出了COM使用1D和 2D NMR和EXAFS光谱。 全蛋白结构金属 结合和RNA结合将与分离的Zn 结合肽（34个氨基酸）。 最后，荧光能量转移 研究将被用来帮助确定三维结构， COM核酸加合物。 这些研究可以提供 翻译激活蛋白结构的关键数据， 提供关于其识别、绑定 并改变其同源RNA的翻译。

Protein control of nucleic acid transcription and translation is basic to all life, but the detailed chemical mechanisms for recognition, binding, and control are poorly understood. A series of experiments is described to study the structure of a translational activating protein, COM, as cloned from bacteriophage Mu, and to study its interactions with its cognate nucleic acid. COM offers a simple paradigm for such proteins. It is a small (62 amino acids), single domain, zinc finger protein. Specific structural studies are proposed for COM using 1D and 2D NMR and EXAFS spectroscopies. the holoprotein structure metal binding and RNA binding will be compared with that of the isolated Zn binding peptide (34 amino acids). Finally, fluorescence energy transfer studies will be used to help define the three-dimensional structure of the COM nucleic acid adduct. Taken together these studies may provide key data on the structure of a translational activating protein and provide the primary data on the mechanisms by which it recognizes, binds, and alters translation of its cognate RNA.