Elucidation of the splicing regulatory function of an intrinsically disordered protein PQBP1
Project/Area Number |
15K07886
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Physical pharmacy
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Research Institution | University of Toyama |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
帯田 孝之 富山大学, 大学院医学薬学研究部(薬学), 准教授 (30578696)
|
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 |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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Keywords | タンパク質 / 天然変性タンパク質 / 相互作用 / アロステリック効果 / SPR / 天然変性蛋白質 / NMR / アロステリック機構 |
Outline of Final Research Achievements |
PQBP1 is composed of a small folded WW domain and a large disordered region. PQBP1 binds to a splicing factor WBP11 and a spliceosomal protein U5-15kD. The hydrophobic area of U5-15kD interacts with the YxxPxxVL motif located in the C-terminal region of PQBP1. In this study, we have shown that the interaction between PQBP1 and U5-15kD is attenuated by the binding of the N-terminal WW domain of PQBP1 to WBP11. Our results also showed that the interaction between U5-15kD and U5-52K strengthen the interaction between U5-15kD and PQBP1.
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Report
(4 results)
Research Products
(4 results)
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[Journal Article] Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD2016
Author(s)
Mizuguchi, M., Obita, T., Kajiyama, A., Kozakai, Y., Nakai, T., Nabeshima, Y., Okazawa, H.
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Journal Title
FEBS Letters
Volume: 590
Issue: 14
Pages: 2221-31
DOI
Related Report
Peer Reviewed
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