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大肠杆菌单链DNA结合蛋白与recA蛋白和单链DNA稳定复合物的持续结合。

Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA.

作者信息

Morrical S W, Lee J, Cox M M

出版信息

Biochemistry. 1986 Apr 8;25(7):1482-94. doi: 10.1021/bi00355a003.

DOI:10.1021/bi00355a003
PMID:2939874
Abstract

The single-stranded DNA binding protein of Escherichia coli (SSB) stimulates recA protein promoted DNA strand exchange reactions by promoting and stabilizing the interaction between recA protein and single-stranded DNA (ssDNA). Utilizing the intrinsic tryptophan fluorescence of SSB, an ATP-dependent interaction has been detected between SSB and recA-ssDNA complexes. This interaction is continuous for periods exceeding 1 h under conditions that are optimal for DNA strand exchange. Our data suggest that this interaction does not involve significant displacement of recA protein in the complex by SSB when ATP is present. The properties of this interaction are consistent with the properties of SSB-stabilized recA-ssDNA complexes determined by other methods. The data are incompatible with models in which SSB is displaced after functioning transiently in the formation of recA-ssDNA complexes. A continuous association of SSB with recA-ssDNA complexes may therefore be an important feature of the mechanism by which SSB stimulates recA protein promoted reactions.

摘要

大肠杆菌的单链DNA结合蛋白（SSB）通过促进和稳定recA蛋白与单链DNA（ssDNA）之间的相互作用，刺激recA蛋白促进的DNA链交换反应。利用SSB的固有色氨酸荧光，已检测到SSB与recA-ssDNA复合物之间存在ATP依赖性相互作用。在DNA链交换的最佳条件下，这种相互作用可持续超过1小时。我们的数据表明，当存在ATP时，这种相互作用并不涉及复合物中recA蛋白被SSB大量取代。这种相互作用的特性与通过其他方法确定的SSB稳定的recA-ssDNA复合物的特性一致。这些数据与SSB在recA-ssDNA复合物形成过程中短暂发挥作用后被取代的模型不相符。因此，SSB与recA-ssDNA复合物的持续结合可能是SSB刺激recA蛋白促进反应机制的一个重要特征。

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Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA.大肠杆菌单链DNA结合蛋白与recA蛋白和单链DNA稳定复合物的持续结合。
Biochemistry. 1986 Apr 8;25(7):1482-94. doi: 10.1021/bi00355a003.
2
Stabilization of recA protein-ssDNA complexes by the single-stranded DNA binding protein of Escherichia coli.大肠杆菌单链DNA结合蛋白对recA蛋白-ssDNA复合物的稳定作用。
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Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction.大肠杆菌单链结合蛋白（SSB）对大肠杆菌重组蛋白A（RecA）与单链DNA结合的影响。竞争性结合的证明及特定蛋白质-蛋白质相互作用的缺失。
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Biochemical properties of the Escherichia coli recA430 protein. Analysis of a mutation that affects the interaction of the ATP-recA protein complex with single-stranded DNA.大肠杆菌recA430蛋白的生化特性。对影响ATP-recA蛋白复合物与单链DNA相互作用的一个突变的分析。
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Direct evidence of the role of ATPγS in the binding of single-stranded binding protein (Escherichia coli) and RecA to single-stranded DNA.直接证据表明，三磷酸鸟苷γS 在单链结合蛋白（大肠杆菌）和 RecA 与单链 DNA 结合中的作用。
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Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein.大肠杆菌基因重组中的蛋白质相互作用。涉及RecO和RecR的相互作用克服了单链DNA结合蛋白对RecA的抑制作用。
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