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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Arrangement of RecA protein in its active filament determined by polarized-light spectroscopy
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Arrangement of RecA protein in its active filament determined by polarized-light spectroscopy

机译：偏光光谱法测定RecA蛋白在其活性丝中的排列

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摘要

Linear dichroism (LD) polarized-light spectroscopy is used to determine the arrangement of RecA in its large filamentous complex with DNA, active in homologous recombination. Angular orientation data for two tryptophan and seven tyrosine residues, deduced from differential LD of wild-type RecA vs. mutants that were engineered to attenuate the UV absorption of selected residues, revealed a rotation by some 40° of the RecA subunits relative to the arrangement in crystal without DNA. In addition, conformational changes are observed for tyrosine residues assigned to be involved in DNA binding and in RecA-RecA contacts, thus potentially related to the global structure of the filament and its biological function. The presented spectroscopic approach, called "Site-Specific Linear Dichroism" (SSLD), may find forceful applications also to other biologically important fibrous complexes not amenable to x-ray crystallographic or NMR structural analysis.
机译：线性二色性（LD）偏振光光谱法用于确定RecA在其具有DNA的大型丝状复合物中的排列，该复合物在同源重组中具有活性。从野生型RecA对突变体的差异LD推导得出的两个色氨酸和七个酪氨酸残基的角取向数据表明，突变体经工程改造以减弱选定残基的紫外线吸收，显示相对于排列而言，RecA亚基旋转了约40°没有DNA的晶体中。另外，观察到酪氨酸残基的构象变化，该酪氨酸残基被指定参与DNA结合和RecA-RecA接触，因此可能与细丝的整体结构及其生物学功能有关。提出的光谱方法，称为“特定于站点的线性二向色性”（SSLD），可能会发现对不适合X射线晶体学或NMR结构分析的其他生物学上重要的纤维复合物也有强大的应用。

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