2012 Fiscal Year Final Research Report
Structure-activity relationship and thermostability of ribonucleoprotein enzyme
| Project/Area Number |
22380062
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
KIMURA Makoto 九州大学, 農学研究院, 教授 (10204992)
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| Co-Investigator(Kenkyū-buntansha) |
GODA Syuichirou 長崎大学, 工学部, 准教授 (00346587)
YAMASHITA Shoji 九州大学, 大学院・農学研究院, 教授 (70089936)
KAKUTA Yoshimitsu 九州大学, 大学院・農学研究院, 准教授 (00314360)
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| Project Period (FY) |
2010 – 2012
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| Keywords | 酵素利用学 / リボザイム |
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| Research Abstract |
The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshiicomprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the proteins, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assayssuggests that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding. Moreover, Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 x 107M-1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA approximately with an equal affinity. On the basis of the results, it was suggested that the simultaneous binding of PhoRpp38 to SL1 and SL2 makes an appropriate orientation of the S and C domains and that PhoRpp38 binding stabilizes base pairing, which increases base staking in PhopRNA
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[Journal Article] Crystal structure of the branching enzyme I (BEI) from Oryza sativaL with implications for catalysis and substrate binding2011
Author(s)
J. Noguchi, K. Chaen, N.T. Vu, T. Akasaka, H. Shimada, T. Nakashima, A. Nishi, H. Satoh, T. Omori, Y. Kakuta, and M. Kimura
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Journal Title
Glycobiology
Volume: 21
Pages: 1108-1116
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