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Cloning and Characterization of a Coronatine-Regulated Tyrosine Aminotransferase from Arabidopsis
Author(s) -
Anna Lopukhina,
Marcus Dettenberg,
Elmar W. Weiler,
Heike HolländerCzytko
Publication year - 2001
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.126.4.1678
Subject(s) - coronatine , arabidopsis , jasmonic acid , tyrosine aminotransferase , biochemistry , biology , complementary dna , arabidopsis thaliana , phytotoxin , gene , tyrosine , enzyme , toxin , mutant , enzyme inducer
In plants, the phytotoxin coronatine, which is an analog of the octadecanoids 12-oxo-phytodienoic acid and/or jasmonic acid, gives rise to a number of physiological responses similar to those of octadecanoids. To further elucidate the physiological role of these compounds, the differential RNA display technique was used to isolate a number of novel octadecanoid-inducible genes expressed in coronatine-treated Arabidopsis. Among these, a cDNA clone was identified that was similar to known tyrosine aminotransferases (TATs). The function was verified with the expressed recombinant protein. In Arabidopsis, the protein is present as a multimer of 98 kD, with a monomer of an apparent molecular mass of 47 kD. TAT mRNA could be induced within 2 h by various octadecanoids and by wounding of the plants. Accumulation of the TAT protein and a 5- to 7-fold increase in its enzymatic activity was observed 7 to 9 h after application of octadecanoids, coronatine, or wounding. The potential role of TAT in the defense response to herbivores and pathogens is discussed.

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