Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities
Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities
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DOI：
10.1093/nar/gkp298
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发表时间：
2009-07-01
影响因子：
14.9
通讯作者：
Kurumizaka, Hitoshi
中科院分区：
文献类型：
--
作者：
Morozumi, Yuichi;Takizawa, Yoshimasa;Kurumizaka, Hitoshi
RAD51是一种真核重组酶，它催化同源配对和链交换反应，是同源重组和双链断裂重组修复的重要步骤。另一方面，人类PSF最初被确定为剪接体的一个组成部分，其在RNA加工、转录和DNA重组中的多种功能随后被揭示。在本研究中，我们发现PSF直接与RAD51相互作用。在低RAD51浓度下，PSF显著增强了RAD51介导的同源配对和链交换；然而，相反，在最佳RAD51浓度下，它抑制了这些由RAD51介导的重组反应。缺失分析显示，PSF的n端区域具有RAD51和DNA结合活性，但含有rna识别基序的中心区域既不结合RAD51也不结合DNA。这些结果表明，PSF可能在同源重组和RNA加工中具有双重功能，分别通过其n端和中心区域。
RAD51, a eukaryotic recombinase, catalyzes homologous-pairing and strand-exchange reactions, which are essential steps in homologous recombination and recombinational repair of double strand breaks. On the other hand, human PSF was originally identified as a component of spliceosomes, and its multiple functions in RNA processing, transcription and DNA recombination were subsequently revealed. In the present study, we found that PSF directly interacted with RAD51. PSF significantly enhanced RAD51-mediated homologous pairing and strand exchange at low RAD51 concentrations; however, in contrast, it inhibited these RAD51-mediated recombination reactions at the optimal RAD51 concentration. Deletion analyses revealed that the N-terminal region of PSF possessed the RAD51- and DNA-binding activities, but the central region containing the RNA-recognition motifs bound neither RAD51 nor DNA. These results suggest that PSF may have dual functions in homologous recombination and RNA processing through its N-terminal and central regions, respectively.