Toward a novel method for constructing an artificial ribonucleopeptide enzyme
Project/Area Number |
25620131
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Bio-related chemistry
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Research Institution | Kyoto University |
Principal Investigator |
MORII TAKASHI 京都大学, エネルギー理工学研究所, 教授 (90222348)
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Project Period (FY) |
2013-04-01 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | 人工酵素 / RNAアプタマー / RNA-ペプチド複合体 / ライブラリー / 活性スクリーニング / 基質結合場 / 分子認識能 / 協同的 / 反応モジュール / 基礎結合場 |
Outline of Final Research Achievements |
A novel method for constructing an artificial enzyme by modification of the peptide subunit of ribonucleopeptide (RNP) with a catalytic group was investigated. We have developed a method to construct highly selective receptors for small molecules by using the RNP scaffold. The peptide subunit of RNP can be further functionalized with retaining the original molecular recognition of RNP receptor, for example, modification of the peptide with a fluorophore converts an RNP receptor to a fluorescent RNP sensor. In this study, an RNP library for the screening of catalytic activity was constructed by using an ATP-binding RNA library and a library of peptides modified at the N-terminal with a catalytic group through various kinds of peptide linkers. Screening of the RNP library for a hydrolytic activity afforded RNPs with enhanced activity.
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Report
(3 results)
Research Products
(13 results)
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[Journal Article] Genetically encoded fluorescent thermosensors visualize subcellular thermoregulation in living cells2013
Author(s)
Shigeki Kiyonaka, Taketoshi Kajimoto, Reiko Sakaguchi, Daisuke Shinmi, Mariko Omatsu-Kanbe, Hiroshi Matsuura, Hiromi Imamura, Takenao Yoshizaki, Itaru Hamachi, Takashi Morii, Yasuo Mori
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Journal Title
Nature Methods
Volume: 10
Issue: 12
Pages: 1232-1238
DOI
Related Report
Peer Reviewed
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