| Project/Area Number |
12680666
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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 |
Biophysics
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
SHIRO Yoshitsugu RIKEN Harima Institute,Biophysical Chemistry laboratory, Chief Scientist, 生体物理化学研究室, 主任研究員 (70183051)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAMURA Hiro RIKEN, Biophysical Chemistry laboratory,Senior Research Scientist, 生体物理化学研究室, 先任研究員 (80270594)
PAK Sam yong Yokohama City University Graduate School of Integrated Science,Associated Professor, 大学院・総合理学研究科, 助教授 (20291932)
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| Project Period (FY) |
2000 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2002: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2001: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2000: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Ethylene / Plant Hormone / Two-component system / Histidine kinase / Copper (I) complex / XAFS / Sensor Protein / センサータンパク質 / エチレン受容体 / 二成分情報伝達系 / リン酸移転 / 銅 |
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| Research Abstract |
Ethylene is a plant hormone, which is significantly involved in life cycle of plants. Ethylene exhibits its physiological activities by virtue of binding to its sensor protein, ETR1. ETR1 belongs to the two-component regulatory system in cells, and mainly consists of two functional domain, sensor domain and histidine kinase domain. Most recently, it has been found that the ETR1 sensor domain contains Cu(I). In the present project,we have been trying to obtain the direct evidence that Cu(I) is the ethylene binding site of ETR1. We constructed expression system of the recombinant protein of the ETR1 sensor domain (trans-membrane protein) in E. coli, established it purification procedure, and measured the Cu K-edge XAFS spectra. The spectra is significantly different in the presence and absence of ethylene, showing that ethylene bind to the Cu(I) sitel of ETR1 and causes its coordination structural changes.
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