Structural studies of a common domain between a regulatory complex involved in DNA methylation and SMC complexes for chromosome maintenance
| Project/Area Number |
26440039
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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 | Institute of Physical and Chemical Research |
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Principal Investigator |
KAMADA Katsuhiko 国立研究開発法人理化学研究所, 平野染色体ダイナミクス研究室, 専任研究員 (70360526)
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| Project Period (FY) |
2014-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 蛋白質複合体 / 染色体凝縮 / Ｘ線結晶構造解析 / エピジェネティック / 構造生物学 / 染色体 / 蛋白質間相互作用 / DNAメチル化 / 結晶構造解析 |
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| Outline of Final Research Achievements |
In recent years, many protein complexes involved in epigenetic gene control were genetically identified. Interestingly, a plant-specific protein complex participating in the regulation contains a hinge-like domain commonly found in proteins, which are involved in eukaryotic chromosome condensation. I investigated the structural relationship of the domain found over these two systems. The crystal structure of the hinge domain of the bacterial SMC protein reveals an asymmetric dimer with a half-opened interface, clarifying involvement of the domain for conformational changes of the overall structure within the SMC complex. I also identified minimal components of the plant-specific complex essential for the stable association to aim further structural analysis.
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Report
(5 results)
Research Products
(14 results)
