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Plant Physiol, August 2001, Vol. 126, pp. 1678-1687
Cloning and Characterization of a Coronatine-Regulated Tyrosine
Aminotransferase from Arabidopsis1
Anna
Lopukhina,
Marcus
Dettenberg,
Elmar W.
Weiler, and
Heike
Holländer-Czytko*
Lehrstuhl für Pflanzenphysiologie,
Ruhr-Universität, D-44780 Bochum, Germany
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.
1
This work was supported by the Deutsche
Forschungsgemeinschaft, Bonn, Germany (grant to E.W.W.).
*
Corresponding author; e-mail
Heike.Hollaender-Czytko{at}ruhr-uni-bochum.de; fax
49-234-3214187.
© 2001 American Society of Plant Physiologists
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