|Budget Amount *help
¥92,222,000 (Direct Cost : ¥70,940,000、Indirect Cost : ¥21,282,000)
Fiscal Year 2015 : ¥15,691,000 (Direct Cost : ¥12,070,000、Indirect Cost : ¥3,621,000)
Fiscal Year 2014 : ¥15,691,000 (Direct Cost : ¥12,070,000、Indirect Cost : ¥3,621,000)
Fiscal Year 2013 : ¥19,500,000 (Direct Cost : ¥15,000,000、Indirect Cost : ¥4,500,000)
Fiscal Year 2012 : ¥19,370,000 (Direct Cost : ¥14,900,000、Indirect Cost : ¥4,470,000)
Fiscal Year 2011 : ¥21,970,000 (Direct Cost : ¥16,900,000、Indirect Cost : ¥5,070,000)
|Outline of Final Research Achievements
Arginine methylation is a post-translational modification catalyzed by the protein arginine methyltransferase (PRMT) family. PRMT1, the predominant member, is responsible for most of the arginine methylation in the cell, is ubiquitously expressed. In contrast, much less is known about its closely related family member, PRMT8. PRMT7 has a unique domain structure consisting two tandem core domains.
We determine the structures of PRMT8 and PRMT7. PRMT8 forms novel helical assembly in the crystal. The mutant protein disrupting the helical assembly exhibits a different cellular localization and reduced the methyltransferase activity, suggesting that the higher oligomerization state is necessary for the proper function of PRMT8. The N and C-terminal core domain of PRMT7 formed the hetero core-dimer like structure. SAH was observed only in the N-terminal catalytic domain. The obtained structural feature suggests that C-terminal core domain lacks the function of the methyltransferase activity.