| Project/Area Number |
15K18485
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
Kondo Keiko 京都大学, エネルギー理工学研究所, 研究員 (00707474)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | NMR / TLS/FUS / タンパク質-核酸相互作用 |
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| Outline of Final Research Achievements |
Translocated liposarcoma protein (TLS) plays important role in the regulation of cyclin D1 (CCND1) transcription and telomere lengthening. In the regulation of CCND1, long non-coding RNA (lncRNA) that is transcribed from upstream of CCND1 interacts with TLS. We determined secondary structure of TLS-binding motif in the lncRNA. NMR study showed that RGG3 domain of TLS interacts with single-stranded region of lncRNA.
In the regulation of telomere lengthening, RGG3 recognizes G-quadruplexes of telomeric DNA and TERRA to form ternary complex. We identified guanine residues involved in the interaction with RGG3. Furthermore, Triple-resonance NMR experiments showed that both Phe and Tyr residues can interact with both telomeric DNA and TERRA. However, in the ternary complex, Phe and Tyr residues prefer to interact with telomeric DNA and TERRA, respectively. We proposed that the plastic roles of Phe and Tyr residues are important for efficient formation of the ternary complex.
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