1990 Fiscal Year Final Research Report Summary
Molecular Basis of Auxin Response in Plants
| Project/Area Number |
01540564
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理学
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| Research Institution | Osaka University, Institute of Scientific and Industrial Research |
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Principal Investigator |
SHIMOMURA Shoji Osaka University, Institute of Scientific and Industrial Research Research Assistant, 産業科学研究所, 助手 (90116046)
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| Project Period (FY) |
1989 – 1990
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| Keywords | Auxin / Phytohormone / Receptor / Signal transduction / Transporter |
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| Research Abstract |
Growth of plants has been known to be regulated by several types of endogenous compounds termed phytohormones. The mechanism of signal perception and cellular response to these hormones are still obscure. In this study we planned to analyze the mechanism of signal perception of a pytohormone, auxin. Multiple types of auxin-binding sites have been found in plant cells. These sites were distinguishable in their subcellular localizations and specificities to auxins and antiauxins. Some of these sites may be genuine receptors functioning in the signal perception. The others would be transporters for inter- and intracellular transport of auxin. Enzymes for synthesis and degradation of auxin would also bind auxin with high affinity. We tried to isolate and characterize these binding sites, since it is expected that the functions of these binding sites will be elucidated with these studies. We purified an auxin-binding protein from maize membranes and sequenced its primary structure using cDNA cloning studies. Subcellular fractionation studies suggested that this binding protein may function as an auxin receptor at the cell surface. We planned to construct transgenic plants and examine the effect of mutation in the gene encoding the auxin-binding protein on the cellular response to auxin. For this purpose we chose Arabidopsis thaliana as plant material and succeeded in isolation of the gene encoding the auxin-binding protein. We furthermore solubilized and partially purified an auxin-transport-inhibitor-binding protein to characterize the mechanism of auxin transport.
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