Structures and Functions of the N-terminal Domains of SUMO Ligase PIAS/Siz Family
Project/Area Number |
19570115
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | National Institute of Agrobiological Sciences |
Principal Investigator |
YAMAZAKI Toshimasa National Institute of Agrobiological Sciences, タンパク質機能研究ユニット, ユニット長 (40360458)
|
Co-Investigator(Kenkyū-buntansha) |
神藤 平三郎 独立行政法人農業・食品産業技術総合研究機構, 植物科学研究領域タンパク質機能研究ユニット, 特別研究員 (80138966)
|
Co-Investigator(Renkei-kenkyūsha) |
SHINDO Heisaburo 独立行政法人農業生物資源研究所, タンパク質機能研究ユニット, 外来研究員 (80138966)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2009: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2008: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2007: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 生物物理 / 蛋白質 / 分子認識 / SUMO化翻訳後修飾 / SUMOリガーゼ / DNA結合 / ヒストン認識 / 構造生理学 / 構造生物学 |
Research Abstract |
Post-translational modification of target proteins by SUMO regulates a wide variety of cellular functions. Among three enzymes (E1, E2 and E3) involved in the SUMO pathway, SUMO E3 ligases are thought to play important roles to recognize target proteins and facilitate their sumoylation. Here, we studied structures and functions of the N-terminal SAP and PHD of SUMO ligase PIAS/Siz family by NMR spectroscopy.
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Report
(4 results)
Research Products
(8 results)