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Fission Yeast Mog1p Homologue, Which Interacts With the Small GTPase Ran, Is Required for Mitosis-to-Interphase Transition and poly(A)+ RNA Metabolism
K. Tatebayashia, T. Tanib,c, and H. Ikedaa,da Department of Molecular Biology, Institute of Medical Science, the University of Tokyo, P.O. Takanawa, Tokyo 108-8639, Japan,
b Department of Biology, Graduate School of Science, Kyushu University, Fukuoka 812-8581, Japan,
c PRESTO, Japan Science and Technology Corporation, Fukuoka 812-8581, Japan
d Microbial Chemistry, Center for Basic Research, The Kitasato Institute, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8642, Japan
Corresponding author: K. Tatebayashi, Department of Molecular Biology, Institute of Medical Science, the University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan., tategone{at}ims.u-tokyo.ac.jp (E-mail)
Communicating editor: F. WINSTON
mog1 mutation in S. cerevisiae, the mog1-1 mutation causes nucleolar accumulation of poly(A)+ RNA at the restrictive temperature in S. pombe, but the signals do not overlap with the fibrillarin-rich region of the nucleolus. Thus, we found that mog1+ is required for the mitosis-to-interphase transition and a class of RNA metabolism. In our attempt to identify suppressors of mog1-1, we isolated the spi1+ gene, which encodes the fission yeast homologue of Ran. We found that overexpression of Spi1p rescues the S. pombe
mog1 cells from death. On the basis of these results, we conclude that mog1+ is involved in the Ran-GTPase system.
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