2023 Fiscal Year Final Research Report
Elucidation of the structure and function common to two intrinsically disordered proteins with significantly different sequences.
| Project/Area Number |
20K06527
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Review Section |
Basic Section 43020:Structural biochemistry-related
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| Research Institution | Japan Atomic Energy Agency (2023)
Rikkyo University (2020-2022) |
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Principal Investigator |
Oda Takashi 国立研究開発法人日本原子力研究開発機構, 原子力科学研究部門 J－PARCセンター, 研究職 (00573164)
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| Project Period (FY) |
2020-04-01 – 2024-03-31
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| Keywords | 天然変性タンパク質 / X線小角散乱 / 古細菌 |
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| Outline of Final Research Achievements |
We predicted that two naturally denatured proteins (IDPs) that are homologous but have significantly different amino acid sequences share a common function. In this study, we aimed to prove this prediction and elucidate the structural features that enable it to perform its functions. We conducted research on such two IDPs. As a result, we showed that both IDPs bind to both DNA and DNA clamp and have a common function of suppressing the sliding of DNA clamp. Initially, we predicted that a common secondary structural motif (α-helix) would be conserved in the two IDPs to exert this function. However, our results suggest that flexible interactions with DNA due to structural flexibility are more important than secondary structural motifs.
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| Free Research Field |
構造生物学
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| Academic Significance and Societal Importance of the Research Achievements |
一般に、タンパク質の機能に重要な領域はアミノ酸配列や立体構造が保存されていると考えられる。しかし、天然変性タンパク質(または天然変性領域)は生物種間でアミノ酸配列保存性が低く、特定の立体構造も取らないため、上記の概念に反する。本研究では、そのような天然変性タンパク質であっても共通の機能を持ちうることを発見した。本研究の成果は他のタンパク質においても従来「重要でない」として見過ごされてきた領域に新たな機能を発見するきっかけとなり、天然変性領域の構造・機能の理解に貢献すると期待する。
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