| Project/Area Number |
16H06693
|
|---|
| Research Category |
Grant-in-Aid for Research Activity Start-up
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Biomolecular chemistry
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
Nakakido Makoto 東京大学, 大学院工学系研究科(工学部), 助教 (80784511)
|
|---|
| Project Period (FY) |
2016-08-26 – 2018-03-31
|
| Project Status |
Completed (Fiscal Year 2017)
|
| Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
|---|
| Keywords | 分子認識 / 多重特異性 / メチル基転移酵素 / 相互作用 / 物理化学 / 蛋白質 / 酵素 / 翻訳後修飾 |
|---|
| Outline of Final Research Achievements |
In this study, we aimed to reveal the molecular mechanism how a multi-specific enzyme recognizes its substrate. We selected SMYD2, a methyltransferase which has methylation activity to a variety of substrates including histone and non-histone proteins, as a model protein. We prepared SMYD2, its substrate p53, and several SMYD2 mutants with mutations on amino acid residues that are supposed to be involved in substrate recognition as recombinant protein and conducted the analysis of the interaction between SMYD2 wild-type/mutants and p53. Though the analyses, we quantitatively described the contribution of each amino acid residue on substrate recognition.
|
