Transport of metal ions-Structural and functional analysis of a novel metal transporter
| Project/Area Number |
12640631
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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 |
植物生理
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| Research Institution | Shizuoka University |
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Principal Investigator |
SHIOI Yuzo Shizuoka University Professor, 理学部, 教授 (70094092)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2001: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2000: ¥2,600,000 (Direct Cost: ¥2,600,000)
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| Keywords | Metal-binding substance / Mg-dechelating substance / Mg-releasing protein / Chlorophyll degradation / Metal transport / クロロフィル分解 |
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| Research Abstract |
In this study, we investigated on Mg-dechelation reaction using artificial substrate, Mg-chlorophyllin, instead of true substrate, chlorophyllide a. During this study, an involvement of Mg-dechelating proteins in addition to the Mg-dechelating substance (MCS) was found. Here, we report the results of this study. The results revealed the presence of at least three isozymes which have Mg-releasing ability. We designated these proteins as Mg-releasing protein (MRP) and purification and characterization of these proteins were carried. Molecular weight of two proteins was estimated to be 20 k and 43 k. The enzyme reaction was strongly inhibited by free radical scavengers as similar to horseradish peroxidase. Absorption spectrum of MRP was, however, very different from that of horseradish peroxidase. The Mg-releasing protein had no activity for chlorophyllide a, a true substrate. It is likely to conclude that MRPs involve Mg-releasing and /or transport, but they are different from Mg-dechelatase that participates releasing of Mg in the chlorophyll degradation pathway. We are now studying on the MRP having 43 k and one another isozymes and cloning of MRP gene.
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Report
(3 results)
Research Products
(16 results)
