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MBC in Press, published online ahead of print March 15, 2006
Mol. Biol. Cell 10.1091/mbc.E05-09-0893

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Submitted on September 26, 2005
Revised on February 15, 2006
Accepted on March 2, 2006

Nuclear RanGAP Is Required for the Heterochromatin Assembly and Is Reciprocally Regulated by Histone H3 and Clr4 Histone Methyltransferase in Schizosaccharomyces pombe

Hitoshi Nishijima,*{dagger} Jun-ichi Nakayama,{ddagger} Tomoko Yoshioka,* Ayumi Kusano,* Hideo Nishitani,* Kei-ichi Shibahara,{dagger} and Takeharu Nishimoto*

*Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan; {dagger}Department of Integrated Genetics, National Insitute of Genetics, Mishima, Shizuoka 411-8540, Japan; {ddagger}Laboratory for Chromatin Dynamics, Center for Developmental Biology, RIKEN, Kobe 650-0047, Japan

Monitoring Editor: Karsten Weis

Although the Ran GTPase activating protein, RanGAP, mainly functions in the cytoplasm, several lines of evidence indicate a nuclear function of RanGAP. We found that Schizosaccharomyces pombe RanGAP, SpRna1, bound the core of histone H3 (H3) and enhanced Clr4-mediated H3-lysine 9 (K9) methylation. This enhancement was not observed for methylation of the H3-tail containing K9 and was independent of SpRna1-RanGAP activity, suggesting that SpRna1 itself enhances Clr4-mediated H3-K9 methylation via H3. Although most SpRna1 is in the cytoplasm, some cofractionated with H3. Sprna1ts mutations caused decreases in Swi6-localization and H3-K9 methylation at all three heterochromatic regions of S. pombe. Thus, nuclear SpRna1 appears to be involved in heterochromatin assembly. All core histones bound SpRna1 and inhibited SpRna1-RanGAP activity. In contrast, Clr4 completely abolished the inhibitory effect of H3 on the RanGAP activity of SpRna1, but partially affected the other histones. SpRna1 formed a trimeric complex with H3 and Clr4, suggesting that nuclear SpRna1 is reciprocally regulated by histones especially H3, and Clr4 on the chromatin to function for higher-order chromatin assembly. We also found that SpRna1 formed a stable complex with Xpo1/Crm1 plus Ran-GTP, in the presence of H3.

Address correspondence to: Takeharu Nishimoto (tnishi{at}molbiol.med.kyushu-u.ac.jp)




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T. Ohba, H. Nishijima, H. Nishitani, and T. Nishimoto
Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts with Ran GTPase and modulates both RanGEF and RanGAP activities.
Genes Cells, June 1, 2008; 13(6): 571 - 582.
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