2013 Fiscal Year Final Research Report
Roles of Multiple-Binding Sites of Conjugating Enzyme E2 in SUMOylation
| Project/Area Number |
23570151
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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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| Research Field |
Structural biochemistry
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| Research Institution | National Institute of Agrobiological Sciences |
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Principal Investigator |
TOSHIMASA Yamazaki 独立行政法人農業生物資源研究所, 生体分子研究ユニット, ユニット長 (40360458)
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| Co-Investigator(Renkei-kenkyūsha) |
FUJIMOTO Zui 独立行政法人農業生物資源研究所 (20370679)
SUZUKI Rintaro 独立行政法人農業生物資源研究所 (00399429)
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| Project Period (FY) |
2011 – 2013
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| Keywords | 生物物理 / 蛋白質 / 分子認識 / 構造生物学 / SUMO化翻訳後修飾 / SUMO化酵素 |
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| Research Abstract |
Post-translational modification of proteins by a small ubiquitin-related modifier (SUMO) regulates many important celluar pathways. SUMOylation requires the sequential action of E1 (activating enzyme), E2 (conjugating enzyme) and often needs E3 (ligases) that mediate substrate specificity for SUMO conjugation. In this process, the transfer mechanism of SUMO from E1 to E2 has not been well clarified. In this study, to reveal the functional roles of interaction network among E1, E2 and SUMO, we performed structural analyses on E2, SUMO, and E2-binding domain (UFD) of E1 from rice, and identified that E2 has multiple SUMO-binding sites with distinct affinities as well as a single UFD-binding site.
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