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首页> 外文期刊>Journal of Molecular Biology >[L29M] substitution in the interface of subunit-subunit interactions enhances Escherichia coli RecA protein properties important for its recombinogenic activity
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[L29M] substitution in the interface of subunit-subunit interactions enhances Escherichia coli RecA protein properties important for its recombinogenic activity

机译：亚基-亚基相互作用界面中的[L29M]取代增强了大肠杆菌RecA蛋白的性质，对其重组活性具有重要意义

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摘要

Genetic analysis of RecA protein chimeras and their ancestors, RecAEc (from Escherichia coli) and RecAPa (Pseudomonas aeruginosa) had allowed us to place these proteins with respect to their recombinogenic activities in the following order: RecAPa > RecAX21 > RecAX20 = RecAEc. While RecAX20 differs from RecAEc in five amino acid residues with two substitutions ([S25A] and [I26V]) at the interface of subunit interactions in the RecA polymer, RecAX20 and RecAX21 differ only by a single substitution [L29M] present at the interface. Here, we present an analysis of the biochemical properties considered important for the recombinogenic activity of all four RecA proteins. While RecAX20 was very similar to RecAEc by all activities analysed, RecAX21 differed from RecAEc in several respects. These differences included an increased affinity for double-stranded DNA, a more active displacement of SSB protein from single-stranded DNA (ssDNA), a decreased end-dependent RecAX21 protein dissociation from a presynaptic complex, and a greater accumulation of intermediate products relative to the final product in the strand-exchange reaction. RecAPa was more tolerant than RecAX21 only to the end-dependent RecA protein dissociation. In addition, RecAPa was more resistant to temperature and salt concentrations in its ability to form a presynaptic RecAPa::ATP::ssDNA filament. Calculations of conformational energy revealed that the [L29M] substitution in RecAX21 polymer caused an increase in its flexibility. This led us to conclude that even a small change in the flexibility of the RecA presynaptic complex could profoundly affect its recombinogenic properties.
机译：通过对RecA蛋白嵌合体及其祖先RecAEc（来自大肠杆菌）和RecAPa（铜绿假单胞菌）进行遗传分析，我们可以按照以下顺序将这些蛋白按照其重组活性进行排列：RecAPa> RecAX21> RecAX20 = RecAEc。虽然RecAX20与RecAEc在五个氨基酸残基上不同，但在RecA聚合物的亚基相互作用界面上有两个取代（[S25A]和[I26V]），而RecAX20和RecAX21的区别仅在于界面上存在一个取代基[L29M]。在这里，我们提出了对所有四种RecA蛋白的重组活性均重要的生化特性的分析。通过分析所有活动，RecAX20与RecAEc非常相似，但RecAX21在某些方面与RecAEc不同。这些差异包括对双链DNA的亲和力增加，单链DNA（ssDNA）中SSB蛋白的更活跃置换，从突触前复合物中解离的末端依赖性RecAX21蛋白减少，中间产物相对于链交换反应中的最终产物。 RecAPa比RecAX21更能耐受末端依赖的RecA蛋白解离。另外，RecAPa具有形成突触前RecAPa :: ATP :: ssDNA细丝的能力，对温度和盐浓度更具抵抗力。构象能的计算表明，RecAX21聚合物中的[L29M]取代引起其柔性的增加。这使我们得出结论，即使RecA突触前复合物的柔韧性发生很小的变化，也可能深刻影响其重组原性。

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