21 プロトポルフィリノーゲン酸化酵素阻害型除草剤耐性タバコ培養細胞の耐性機構の解明

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Protoporphyrinogen oxidase (Protox) is the last common enzyme in the chlorophyll and heme biosynthesis pathways. In plants, two isoenzymes of Protox are located in chloroplasts and mitochondria, respectively. Protox is also known as the target enzyme of phtalimide compounds such as S23142. We have previously obtained S23142-resistant tobacco cultured cells (YZI-1S) by the stepwise selection of the herbicide. Recent our several line of data suggested that the herbicide resistance of YZI-1S cells is due to the overproduction of mitochondrial Protox though primary target site of the herbicide is chloroplast Protox. However, it is still unclear whether the overaccumulation of mitochondrial Protox involved with increment of the enzymatic activity is acctually occured, and whether the overaccumulation of mitochondrial Protox causes the tolerance to S23142, in YZI-1S cells. To elucidate the molecular mechanism of the herbicide resistance in YZI-1S cells, we examined the protein accumulation, enzymatic activity, and the inhibition of Protox activity by S23142. Immunoblot analysis showed that the accumulation of plastidal Protox protein was apparently the same in both wild type and YZI-1S cells, whereas the accumulation of mitochondrial Protox protein YZI-1S cells was much higher than that of wild type cells. The increment of Protox activity and the decrease of IC_<50> value to S23142 were detected only in mitochondrial fraction from YZI-1S cells. These results clearly indicated that the herbicide resistance of YZI-1S cells in due to the overproduction of mitochondrial Protox.
植物化学調節学会の論文
2000-11-02

21 プロトポルフィリノーゲン酸化酵素阻害型除草剤耐性タバコ培養細胞の耐性機構の解明

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