A functional study on the tRNA mimicry complexes in genetic decoding.
Project/Area Number |
23657071
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | The University of Tokyo |
Principal Investigator |
ITO Koichi 東京大学, 新領域創成科学研究科, 教授 (10262073)
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Project Period (FY) |
2011 – 2012
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Project Status |
Completed (Fiscal Year 2013)
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Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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Keywords | タンパク質合成 / tRNA分子擬態 / 遺伝暗号 / mRNA品質管理 / Gタンパク質 / リボソーム / 翻訳終結 / 翻訳調節 / タンパクs質合成 |
Research Abstract |
In order to elucidate the molecular characteristics of tRNA-mimicking proteins involved in genetic decoding and mRNA surveillance, we have conducted following experiments. (i) Structural and Biochemical analyses for the complexes of omnipotent archaeal translation elongation factor (aEF1alpha) with tRNA mimicry proteins (aRF1, aPelota). (ii) Genetic analyses for the functionality of tRNA-mimicking complex on the ribosome. These analyses revealed that the specific regions are located in the binding interface of the tRNA-mimicking complexes and that a novel functional site adjacent to the codon recognition site, on the tip domain that mimics the tRNA anticodon-loop is crucial for their functionality. These novel domains likely participate in decoding and mRNA surveillance, coupled with the GTPase switch function on the ribosome.
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Report
(4 results)
Research Products
(28 results)
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[Journal Article] Single molecule imaging of the trans-translation entry process via anch oring of the tagged ribosome.2011
Author(s)
Zhou, Z-P., Shimizu, Y., Tadakuma, H.*, Taguchi, H., Ito, K., Ueda, T.
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Journal Title
J. Biochem.
Volume: 149
Issue: 5
Pages: 609-618
DOI
NAID
Related Report
Peer Reviewed
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