Association of human RAD52 protein with transcription factors
Association of human RAD52 protein with transcription factors
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DOI：
10.1016/s0006-291x(02)02353-7
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发表时间：
2002-10-11
影响因子：
3.1
通讯作者：
Shen, ZY
中科院分区：
文献类型：
--
作者：
Liu, JM;Meng, XB;Shen, ZY
人RAD 52蛋白参与DNA同源重组。已经鉴定了四个主要的功能结构域：DNA结合结构域（氨基酸1-85）、自缔合和UBC 9相互作用结构域（氨基酸85-159）、RPA相互作用结构域（氨基酸221-280）和RAD 51相互作用结构域（氨基酸287-330）。然而，它是不确定的C-末端区域的功能作用的RAD 52蛋白。在这份报告中，我们证明了协会的C-末端结构域的人RAD 52（氨基酸302-418）与XPB和XPD亚基的转录因子TFIIH和RNA聚合酶II（RNAPII）。使用Gal-4结合为基础的转录测定，我们进一步表明，该C-末端结构域激活转录。然而，RAD 52自缔合结构域抑制转录，导致全长RAD 52蛋白的转录抑制的总体活性。这些结果表明，一种新的活性的RAD 52在转录调控，并可能进一步暗示功能作用的RAD 52靶向DNA损伤的转录活性位点的重组修复。(C)2002 Elsevier Science（美国）。All rights reserved.
The human RAD52 protein has been implicated in DNA homologous recombination. Four major functional domains have been identified: a DNA binding domain (amino acids 1-85), a self-association and UBC9-interacting domain (amino acids 85-159), an RPA-interacting domain (amino acids 221-280), and a RAD51-interacting domain (amino acids 287-330). However, it is uncertain about the functional roles of the C-terminal region of RAD52 protein. In this report, we demonstrate an association of a C-terminal domain of human RAD52 (amino acids 302-418) with the XPB and XPD subunits of transcription factor TFIIH and RNA polymerase II (RNAPII). Using a Gal-4 binding based transcription assay, we further show that this C-terminal domain activates transcription. However, the RAD52 self-association domain suppresses transcription, resulting in an overall activity of transcriptional suppression by the full-length RAD52 protein. These results suggest a novel activity of RAD52 in transcription regulation and may further imply a functional role of RAD52 in targeting DNA damage on transcription active loci to recombinational repair. (C) 2002 Elsevier Science (USA). All rights reserved.