Engineerability of a functional ribonucleoprotein complex
Project/Area Number |
23550190
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Chemistry related to living body
|
Research Institution | Tokyo Gakugei University |
Principal Investigator |
HARADA Kazuo 東京学芸大学, 教育学部, 教授 (00301169)
|
Project Period (FY) |
2011 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | リボヌクレオタンパク質複合体 / λNタンパク質 / アンチターミネーション / リボヌクレオタンパク質(RNP)複合体 / RNA-ペプチド複合体 / リボヌクレオタンパク質(RNP)複合体 |
Research Abstract |
In order to understand the molecular basis for ribonucleoprotein (RNP) structure and function, we attempted the engineering of the interactions and the spatial organization of the N antitermination complex. Relatively small changes in the spatial orientation of the RNA site have been shown to result in large changes in antitermination activity. We found that it is possible to partially recover activity lost upon altering the orientation of the core HIV RRE site within the antitermination complex by simultaneously modifiyng the orientation of RNA elements and N protein domains. We also showed that optimization of the interaction of N protein with NusA and RNA polymerase lead to a partial recovery of antitermination activity. The results show that the spatial orientation of the core interaction within the antitermination complex can be engineered in a rational manner, demonstrating the engineerability of ribonucleoprotein complexes.
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Report
(4 results)
Research Products
(9 results)