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J. Biol. Chem., Vol. 281, Issue 12, 8153-8160, March 24, 2006

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Requirement of the Protein B23 for Nucleolar Disassembly Induced by the FRGY2a Family Proteins^*

From the Stem Cell Institute, Division of Hematology, Oncology and Transplantation, Department of Medicine, University of Minnesota, Minneapolis, Minnesota 55455

In Xenopus somatic cell nuclear cloning, the nucleoli of donor nuclei rapidly and almost completely disappear in egg cytoplasm. We previously showed that the germ cell-specific proteins FRGY2a and FRGY2b were responsible for this unusually drastic nucleolar disassembly. The nucleolar disassembly occurs without inhibition of pre-rRNA transcription, a well known trigger for nucleolar segregation, and the mechanism for the nucleolar disassembly by FRGY2a and FRGY2b remains largely unknown. In this study, we searched for FRGY2a-interacting proteins and investigated the functional consequences of their interactions through a series of experiments. We showed that during the nucleolar disassembly, FRGY2a localized to the nucleoli of isolated nuclei and was capable of disassembling purified nucleoli, suggesting a direct interaction between FRGY2a and nucleolar components. Using a His tag pulldown approach, we identified the abundant and multifunctional nucleolar protein B23 as a potential target of FRGY2a and its related human protein YB1. A specific interaction between FRGY2a/YB1 and B23 was confirmed by co-immunoprecipitation. Finally, B23 knockdown using short interfering RNA and a subsequent add-back experiment confirmed that B23 was necessary for nucleolar disassembly by YB1. We propose that FRGY2a and YB1 disassemble nucleoli by sequestering B23, which is associated with pre-ribosomes and other structurally important nucleolar components.

Received for publication, December 2, 2005 , and in revised form, January 5, 2006.

^* This work was supported in part by grants from the National Institutes of Health (Grant R01 GM068027), the University of Minnesota Graduate School, and the Minnesota Medical Foundation (to N. K.) The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Dept. of Plastic, Reconstructive and Aesthetic Surgery, Graduate School of Medicine, University of Tokyo, 113-8655, Japan.

² Supported by the Undergraduate Research Opportunity Program.

³ To whom correspondence should be addressed: Stem Cell Institute, Division of Hematology, Oncology and Transplantation, Dept. of Medicine, University of Minnesota, MMC 716, 420 Delaware St. SE, Minneapolis, MN 55455. Tel.: 612-624-0498; Fax: 612-624-2436; E-mail: kikyo001{at}tc.umn.edu.

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