| Project/Area Number |
23659024
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Physical pharmacy
|
|---|
| Research Institution | Hiroshima University |
|---|
Principal Investigator |
TATE Shinichi 広島大学, 大学院・理学研究科, 教授 (20216998)
|
|---|
| Project Period (FY) |
2011 – 2012
|
| Project Status |
Completed (Fiscal Year 2012)
|
| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
|---|
| Keywords | 構造生物学 / 過渡的構造形成 / １３C検知 / 安定同位体 / NMR / 天然変性タンパク質 / 蛋白質 / 生体高分子 / 生物物理 |
|---|
| Research Abstract |
We analyzed one of the general transcription factors in yeast cell, Tfa2, with the 13C and 1H detection NMR methods. In this work, we particularly focused on the intrinsically disordered part in Tfa2, which binds to Gal11 subunit in the Mediator complex. The severe signal overlaps typically found for the ID segment were solved using the 13C and 15N evolution axes, whose chemical shifts have significant dispersions over the other nuclear spins in protein.We found the Mediator binding domain of Tfa2, Tfa2-mbd, transiently forms three-helix structure. The transient structure formation was mediated by its homo-dimer formation. We also found that the transiently folded structure has binding ability to Gal11; the mutant that lacks the transient folding ability does not bind to Gal11. Over all, the present research has demonstrated the unique structural and functional properties associated with the ID part in Tfa2.
|
