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J. Biol. Chem., Vol. 280, Issue 7, 5496-5502, February 18, 2005

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Protein NPM3 Interacts with the Multifunctional Nucleolar Protein B23/Nucleophosmin and Inhibits Ribosome Biogenesis^*

Nian Huang, Sandeep Negi, Attila Szebeni, and Mark O. J. Olson

From the Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216

Protein B23/nucleophosmin is a multifunctional protein that plays roles in ribosome biogenesis, control of centrosome duplication, and regulation of p53 expression. A yeast two-hybrid screen was performed in a search for interaction partners of B23. The complementary DNA for a highly acidic protein, nucleoplasmin 3 (NPM3), was found in multiple positive clones. Protein NPM3 and its interaction with B23 were further characterized. Endogenous B23 was able to be co-immunoprecipitated with NPM3, and this complex was resistant to ribonuclease treatment and high concentrations of salt. The N-terminal 35–90 amino acids of B23 were found to be required for their interaction. Separate co-immunoprecipitation studies of B23 and NPM3 suggested the existence of two different complexes, one containing B23 and 28 S ribosomal RNA (rRNA) and another composed of B23, NPM3, and other proteins, but no RNA. NPM3 was localized in the nucleolus, and its nucleolar localization depended on active rRNA transcription. In the cells overexpressing NPM3, there were decreased rates of pre-rRNA synthesis and processing. Overexpression of a mutant of NPM3 that did not interact with B23 did not alter pre-rRNA synthesis and processing, suggesting that the interaction of NPM3 with B23 plays a role in the ribosome biogenesis.

Received for publication, July 12, 2004 , and in revised form, December 13, 2004.

^* This work was supported in part by a grant from the National Science Foundation EPSCoR Protein Structure and Localization Group Project and by the Medical Guardian Society of the University of Mississippi. 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.

To whom correspondence should be addressed. Tel.: 601-984-1500; Fax: 601-984-1501; E-mail: molson{at}biochem.umsmed.edu.

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