Post-translational modification of erythroid-specific 5-aminolevulinate synthase and its' role in erythroid differentiation.
| Project/Area Number |
20590301
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
FURUYAMA Kazumichi Tohoku University, 大学院・医学系研究科, 准教授 (80280874)
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| Co-Investigator(Kenkyū-buntansha) |
SHIBAHARA Shigeki 東北大学, 大学院・医学系研究科, 教授 (00154253)
柴原 茂樹 東北大学, 大学院・医学系研究科, 教授 (70206142)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2010: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2009: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2008: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 分子病態学 / 鉄芽球性貧血 / アミノレブリン酸合成酵素 / 翻訳後修飾 / SUMO / 赤芽球 / ヘム |
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| Research Abstract |
Erythroid-specific 5-aminolevulinate synthase (ALAS2) is the rate-limiting enzyme of heme biosynthetic pathway in erythroid cells. In this project, we have tried to clarify how the expression of ALAS2 is regulated post-translationally in vivo. As a result, we found that ALAS2 formed covalent homo-dimer, which was not able to translocate into mitochondria, depending on the concentration of intracellular heme level in HEK293 cells. Moreover, we have identified that ALAS2 protein could be SUMOylated, when it was co-expressed with E1, E2 enzyme of SUMOylation and SUMO1 (Small Ubiquitin like Modifier 1) in E. coli. These post-translational modifications of ALAS2 protein were hitherto unknown phenomena, thus it should be important to examine how these modifications were involved in the functional regulation of ALAS2 protein, as well as in erythroid differentiation.
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Report
(4 results)
Research Products
(31 results)
