Explanation of assembly mechanism of 5S RNP in eukaryotic ribosome biosynthesis
| Project/Area Number |
25291008
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
YAO Min 北海道大学, 先端生命科学研究科(研究院), 教授 (40311518)
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| Co-Investigator(Renkei-kenkyūsha) |
KOMODA Keisuke 北海道大学, 大学院先端生命科学研究院, 特任助教 (40581640)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥18,070,000 (Direct Cost: ¥13,900,000、Indirect Cost: ¥4,170,000)
Fiscal Year 2015: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥6,110,000 (Direct Cost: ¥4,700,000、Indirect Cost: ¥1,410,000)
Fiscal Year 2013: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
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| Keywords | リボソーム生合成 / 5S RNP / Rrs1 / Rpf2 / 5S rRNA / X線結晶解析 / 相互作用解析 / 5S rRNP |
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| Outline of Final Research Achievements |
Proteins Rpf2 and Rrs1 act as ribosome assembly factors which recruit RpL5, RpL11 and 5S rRNA into pre-90S by formation of 5S RNP complex. In this study, in order to elucidate how Rpf2 and Rrs1 work for maturation of pre-90S, we determinate the Rpf2-Rrs1 core complex from Aspergillus nidulans. The structure contains the tightly interlocked N-terminal domains of Rpf2 and Rrs1. The long-helix of Rrs1 joins the C-terminal half of Rpf2 N-terminal domains as if it is a part of a single molecule. In addition, gel shift analysis of Rpf2-Rrs1 complex and its mutants revealed that the Rpf2-Rrs1 complex binds directly to 5S rRNA with three parts. Based on these studies and previous reports, we propose a model for ribosomal component recruitment to the pre-90S ribosome precursor.
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Report
(4 results)
Research Products
(8 results)
