Study on the mechanism of the ribonucleoprotein complex
Project/Area Number |
19380060
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied biochemistry
|
Research Institution | Kyushu University |
Principal Investigator |
KIMURA Makoto Kyushu University, 大学院・農学研究院, 教授 (10204992)
|
Co-Investigator(Kenkyū-buntansha) |
KAKUTA Yoshimitsu 九州大学, 大学院・農学研究院, 准教授 (00314360)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥20,020,000 (Direct Cost: ¥15,400,000、Indirect Cost: ¥4,620,000)
Fiscal Year 2009: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2008: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2007: ¥10,400,000 (Direct Cost: ¥8,000,000、Indirect Cost: ¥2,400,000)
|
Keywords | リボヌクレアーゼP / tRNA / RNAプロセシング / リボザイム / 結晶構造 / リボ核タンパク質 / 前駆体tRNA / タンパク質結晶構造 / 超好熱古細菌 / 酵素利用学 / RNAシャペロン / リボ核ダンパク質 |
Research Abstract |
Ribonuclease P (RNase P) is composed of a catalytic RNA (PhopRNA) and five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, PhoRpp38). In this study, we determined the crystal structure of the protein complex composed of PhoRpp21 and PhoRpp29. Furthermore, we examined the protein binding sites on PhopRNA by biochemical methods and analyzed the activated structure of RNase P RNA (PhopRNA) in Pyrococcus horikoshii OT3 was characterized by circular dichroism (CD) and ultraviolet (UV) absorbance spectra.
|
Report
(4 results)
Research Products
(36 results)