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MBC in Press, published online ahead of print January 10, 2007
Mol. Biol. Cell 10.1091/mbc.E06-11-1021

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Submitted on November 17, 2006
Revised on December 15, 2006
Accepted on December 29, 2006

Aurora-B Regulates RNA Methyltransferase NSUN2

Shiho Sakita-Suto,* Akifumi Kanda,* Fumio Suzuki,* Sunao Sato,{dagger} Takashi Takata,{dagger} and Masaaki Tatsuka*

*Department of Molecular Radiobiology, Division of Genome Biology, Research Institute for Radiation Biology and Medicine, and {dagger}Department of Oral Maxillofacial Pathobiology, Division of Frontier Medical Science, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8553, Japan

Monitoring Editor: A. Gregory Matera

Disassembly of the nucleolus during mitosis is driven by phosphorylation of nucleolar proteins. RNA processing stops until completion of nucleolar reformation in G1-phase. Here, we describe the RNA methyltransferase NSUN2, a novel substrate of Aurora-B that contains an NOL1/NOP2/sun domain. NSUN2 was concentrated in the nucleolus during interphase, and was distributed in the perichromosome and cytoplasm during mitosis. Aurora-B phosphorylated NSUN2 at Ser139. Nucleolar proteins NPM1/nucleophosmin/B23 and nucleolin/C23 were associated with NSUN2 during interphase. In mitotic cells, association between NPM1 and NSUN2 was inhibited, but NSUN2-S139A was constitutively associated with NPM1. The Aurora inhibitor Hesperadin induced association of NSUN2 with NPM1 even in mitosis, despite the silver staining nucleolar organizer region disassembly. In vitro methylation experiments revealed that the Aurora-B-phosphorylation and the phosphorylation-mimic mutation (S139E) suppressed methyltransferase activities of NSUN2. These results indicate that Aurora-B participates to regulate the assembly of nucleolar RNA-processing machinery and the RNA methyltransferase activity of NSUN2 via phosphorylation at Ser139 during mitosis.

Address correspondence to: Masaaki Tatsuka (haruo{at}hiroshima-u.ac.jp)




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