STRUCTURAL STUDIES OF COM, A VIRAL ZINC-FINGER PROTEIN

核酸转录和翻译的蛋白质控制是基本的 对所有生命来说，除了识别的详细化学机制， 人们对结合和控制知之甚少。一系列的实验是 被描述为研究翻译激活蛋白的结构， Com，并研究其与Mu噬菌体的相互作用。 它的同源核酸。COM为这种情况提供了一个简单的范例 蛋白质。它是一个小的(62个氨基酸)，单一结构域，锌指 蛋白。提出了用一维和一维的方法研究COM的具体结构。 2D核磁共振和EXAFS光谱分析。全蛋白结构金属 结合和RNA结合将与分离的锌进行比较 结合肽(34个氨基酸)。最后，荧光能量转移 研究将用来帮助定义 COM核酸加合物。总而言之，这些研究可能会提供 翻译激活蛋白结构的关键数据和 提供有关其识别、约束、 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.