Molecular mechanism of stop codon recognition by eRF1
| Project/Area Number |
15570104
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | RIKEN (2004)
National Cancer Center Research Institute and Research Center for Innovative Oncology, National Cancer Center Hospital East (2003) |
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Principal Investigator |
MURAMATSU Tomonari RIKEN, Protein Structure Team, Senior Research Scientist, タンパク質構造研究チーム, 上級研究員 (70212256)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2004: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2003: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | eukaryote / protein biosynthesis / stop codon / codon recognition / translation termination / eRF1 / human |
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| Research Abstract |
ETF1/eRF1,which has recently been suggested to be a myeloid tumor suppressor gene, codes for the class-I release factor which recognizes an in-frame stop codon in translation termination processes of gene expression. This proteinaceous factor eRF1(eukaryotic release factor 1) recognizes all of the three stop codons, UAA, UGA and UAG, but not the Trp codon UGG. This discrimination must require some conformational changes in the recognition domain of eRF1,because the UGG codon cannot be eliminated if eRF1 recognizes the stop codons by simply binding to A/G as the 2nd letter and A/G the 3rd. To address the mechanism of stop codon recognition, we prepared ^<15>N-labeled and ^<15>N/^<13>C-labeled codon recognition domains, assigned all ^1H^N and ^<15>N resonances of native non-proline back bone residues, and now are analyzing dynamic structure of this domain by NMR spectroscopy.
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Report
(3 results)
Research Products
(10 results)
