STRUCTURAL STUDIES OF COM, A VIRAL ZINC-FINGER PROTEIN

COM（一种病毒锌指蛋白）的结构研究

• 批准号: 2187592
• 负责人: George L McLendon
• 金额: $ 8.39万
• 依托单位: UNIVERSITY OF ROCHESTER
• 依托单位国家: 美国
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-05-01 至 1995-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2187592
• 关键词: X ray spectrometry; adduct; chemical binding; fluorescent dye /probe; nuclear magnetic resonance spectroscopy; protein structure; translation factor; virus protein; zinc

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.

核酸转录和翻译是蛋白质控制的基础