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• W2020777762 abstract "Abstract Serotonin N ‐acetyltransferase ( SNAT ), the penultimate enzyme in melatonin biosynthesis, catalyzes the conversion of serotonin into N ‐acetylserotonin. Plant SNAT is localized in chloroplasts. To test SNAT localization effects on melatonin synthesis, we generated transgenic rice plants overexpressing a sheep ( Ovis aries ) SNAT ( O a SNAT ) in their chloroplasts and compared melatonin biosynthesis with that of transgenic rice plants overexpressing O a SNAT in their cytoplasm. To localize the O a SNAT in chloroplasts, we used a chloroplast targeting sequence ( CTS ) from tobacco protoporphyrinogen IX oxidase ( PPO ), which expresses in chloroplasts. The purified recombinant CTS : O a SNAT fusion protein was enzymatically functional and localized in chloroplasts as confirmed by confocal microscopic analysis. The chloroplast‐targeted CTS : O a SNAT lines and cytoplasm‐expressed O a SNAT lines had similarly high SNAT enzyme activities. However, after cadmium and butafenacil treatments, melatonin production in rice leaves was severalfold lower in the CTS : O a SNAT lines than in the O a SNAT lines. Notably, enhanced SNAT enzyme activity was not directly proportional to the production of N ‐acetylserotonin, melatonin, or 2‐hydroxymelatonin, suggesting that plant SNAT has a role in the homeostatic regulation of melatonin rather than in accelerating melatonin synthesis." @default.
• W2020777762 created "2016-06-24" @default.
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• W2020777762 date "2015-04-02" @default.
• W2020777762 modified "2023-10-03" @default.
• W2020777762 title "Chloroplastic and cytoplasmic overexpression of sheep serotonin <i>N</i>‐acetyltransferase in transgenic rice plants is associated with low melatonin production despite high enzyme activity" @default.
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• W2020777762 doi "https://doi.org/10.1111/jpi.12231" @default.
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