Co-localization in replication foci and interaction of human Y-family members, DNA polymerase polη and REV1 protein
Co-localization in replication foci and interaction of human Y-family members, DNA polymerase polη and REV1 protein
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DOI：
10.1016/j.dnarep.2004.06.015
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发表时间：
2004-11-02
期刊：
影响因子：
3.8
通讯作者：
Cordonnier, A
中科院分区：
文献类型：
--
作者：
Tissier, A;Kannouche, P;Cordonnier, A
复制性DNA聚合酶沿着复制叉的进程可能会受到基因组中病变的阻碍。规避这些障碍的一种方法涉及募集专门的DNA聚合酶，其在受损位点附近执行有限的核苷酸掺入。这一过程需要DNA聚合酶在复制型和特化型DNA聚合酶之间转换。五种真核生物蛋白质可以在体外进行损伤DNA的跨损伤合成（TLS），DNA聚合酶xi、eta、iota和kappa以及REV 1。为了鉴定与hpoleta相互作用的新蛋白质，我们进行了酵母双杂交筛选。在本文中，我们表明，hREV 1相互作用与hpoleta以及hpolkappa和差与hpoliota。此外，细胞定位分析表明，hREV 1是存在的，与hpoleta在复制工厂在停滞的复制叉，并与核结构紧密相关。这种hREV 1核定位的发生与hpoleta的存在无关。总之，我们的数据表明hREV1作为招募TLS中涉及的DNA聚合酶的支架的核心作用。(C)2004 Elsevier B.V.保留所有权利。
The progress of replicative DNA polymerases along the replication fork may be impeded by the presence of lesions in the genome. One way to circumvent such hurdles involves the recruitment of specialized DNA polymerases that perform limited incorporation of nucleotides in the vicinity of the damaged site. This process entails DNA polymerase switch between replicative and specialized DNA polymerases. Five eukaryotic proteins can carry out translesion synthesis (TLS) of damaged DNA in vitro, DNA polymerases xi,eta,iota, and kappa, and REV1. To identify novel proteins that interact with hpoleta, we performed a yeast two-hybrid screen. In this paper, we show that hREV1 interacts with hpoleta as well as with hpolkappa and poorly with hpoliota. Furthermore, cellular localization analysis demonstrates that hREV1 is present, with hpoleta in replication factories at stalled replication forks and is tightly associated with nuclear structures. This hREV1 nuclear localization occurs independently of the presence of hpoleta. Taken together, our data suggest a central role for hREV1 as a scaffold that recruits DNA polymerases involved in TLS. (C) 2004 Elsevier B.V. All rights reserved.