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首页> 外文期刊>Molecular and Cellular Biology >Sumoylation of the Novel Protein hRIPβ Is Involved in Replication Protein A Deposition in PML Nuclear Bodies
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Sumoylation of the Novel Protein hRIPβ Is Involved in Replication Protein A Deposition in PML Nuclear Bodies

机译：新型蛋白hRIPβ的糖基化参与PML核体内复制蛋白A的沉积。

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Replication protein A (RPA) is a single-stranded-DNA-binding protein composed of three subunits with molecular masses of 70, 32, and 14 kDa. The protein is involved in multiple processes of eukaryotic DNA metabolism, including DNA replication, repair, and recombination. In Xenopus, Xenopus RPA-interacting protein α has been identified as a carrier molecule of RPA into the nucleus. In this study, human RPA-interacting protein α (hRIPα) and five novel splice isoforms (named hRIPα, hRIPβ, hRIPγ, hRIPδ1, hRIPδ2, and hRIPδ3 according to the lengths of their encoding peptides) were cloned. Among hRIP isoforms, hRIPα and hRIPβ were found to be the major splice isoforms and to show different subcellular localizations. While hRIPα localized to the cytoplasm, hRIPβ was found in the PML nuclear body. Modification of hRIPβ by sumoylation was found to be required for localization to the PML nuclear body. The results of the present work demonstrate that hRIPβ transports RPA into the PML nuclear body and releases RPA upon UV irradiation. hRIPβ thus plays an important role in RPA deposition in PML nuclear bodies and thereby supplements RPA for DNA metabolism.
机译：复制蛋白A（RPA）是一种单链DNA结合蛋白，由分子量分别为70、32和14 kDa的三个亚基组成。该蛋白质参与真核DNA代谢的多个过程，包括DNA复制，修复和重组。在非洲爪蟾中，已经确定非洲爪蟾 RPA相互作用蛋白α是RPA进入细胞核的载体分子。在这项研究中，克隆了人类RPA相互作用蛋白α（hRIPα）和五个新的剪接同工型（根据其编码肽的长度命名为hRIPα，hRIPβ，hRIPγ，hRIPδ1，hRIPδ2和hRIPδ3）。在hRIP同工型中，hRIPα和hRIPβ是主要的剪接同工型，并显示出不同的亚细胞定位。虽然hRIPα定位于细胞质，但在PML核体内发现了hRIPβ。发现通过SUMO化来修饰hRIPβ对于定位到PML核体是必需的。本工作的结果表明，hRIPβ将RPA转运到PML核体内，并在紫外线照射下释放RPA。因此，hRIPβ在RML在PML核体中的沉积中起重要作用，从而补充了RPA的DNA代谢。

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