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J. Biol. Chem., Vol. 279, Issue 9, 8343-8350, February 27, 2004

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A Novel Human Nucleolar Protein, Nop132, Binds to the G Proteins, RRAG A/C/D^*

Takeshi Sekiguchi, Yuko Todaka, Yonggang Wang, Eiji Hirose, Nobutaka Nakashima, and Takeharu Nishimoto

From the Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan

RRAG A (Rag A)/Gtr1p is a member of the Ras-like small G protein family that genetically interacts with RCC1, a guanine nucleotide exchange factor for RanGTPase. RRAG A/Gtr1p forms a heterodimer with other G proteins, RRAG C and RRAG D/Gtr2p, in a nucleotide-independent manner. To further elucidate the function of RRAG A/Gtr1p, we isolated a protein that interacts with RRAG A. This protein is a novel nucleolar protein, Nop132. Nop132 is associated with the GTP form, but not the GDP form, of RRAG A, suggesting that RRAG A might regulate Nop132 function. Nop132 is also associated with RRAG C and RRAG D. The Nop132 amino acid sequence is similar to the Saccharomyces cerevisiae nucleolar Nop8p, which is associated with Gtr1p, Gtr2p, and Nip7p. Nop132 also interacts with human Nip7 and is colocalized with RRAG A, RRAG C, and Nip7. RNA interference knockdown of Nop132 inhibited cell growth of HeLa cells.

Received for publication, June 5, 2003 , and in revised form, November 13, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB109030.

^* This work was supported by Grants-in-aid for Specially Promoted Research (to T. N.) and by a Grant-in-aid for Scientific Research on Priority Areas (to T. S.), from the Japan Ministry of Education, Science, Sport and Culture. 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.

Present address: National Institute of Advanced Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-higashi, Toyohira-ku, Sapporo 062-8517, Japan.

To whom correspondence should be addressed. Tel.: 81-92-642-6177; Fax: 81-92-642-6183; E-mail: sekigu{at}molbiol.med.kyushu-u.ac.jp.

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