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Sumoylation of the Novel Protein hRIPß Is Involved in Replication Protein A Deposition in PML Nuclear Bodies

Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejon 305-701, South Korea

Received 24 January 2005/ Returned for modification 28 February 2005/ Accepted 15 June 2005

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 has been identified as a carrier molecule of RPA into the nucleus. In this study, human RPA-interacting protein (hRIP) and five novel splice isoforms (named hRIP, hRIPß, hRIP, hRIP1, hRIP2, and hRIP3 according to the lengths of their encoding peptides) were cloned. Among hRIP isoforms, hRIP and hRIPß were found to be the major splice isoforms and to show different subcellular localizations. While hRIP localized to the cytoplasm, hRIPß was found in the PML nuclear body. Modification of hRIPß by sumoylation was found to be required for localization to the PML nuclear body. The results of the present work demonstrate that hRIPß transports RPA into the PML nuclear body and releases RPA upon UV irradiation. hRIPß thus plays an important role in RPA deposition in PML nuclear bodies and thereby supplements RPA for DNA metabolism.

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