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Isolation of a glucosyltransferase from Arabidopsis thaliana active in the metabolism of the persistent pollutant 3,4‐dichloroaniline
Author(s) -
Loutre Caroline,
Dixon David P.,
Brazier Melissa,
Slater Malcolm,
Cole David J.,
Edwards Robert
Publication year - 2003
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2003.01742.x
Subject(s) - arabidopsis , biology , arabidopsis thaliana , biochemistry , glucosyltransferase , enzyme , phenols , gene , mutant
Summary The pollutant 3,4‐dichloroaniline (DCA) was rapidly detoxified by glucosylation in Arabidopsis thaliana root cultures, with the N‐ β‐ d ‐glucopyranosyl‐DCA exported into the medium. The N ‐glucosyltransferase ( N‐ GT) responsible for this activity was purified from Arabidopsis suspension cultures and the resulting 50 kDa polypeptide analysed by matrix‐assisted laser desorption ionization time of flight mass spectrometry (MALDI‐TOF MS) following tryptic digestion. The protein was identified as GT72B1. The GT was cloned and the purified recombinant enzyme shown to be highly active in conjugating DCA and 2,4,5‐trichlorophenol, as well as several other chlorinated phenols and anilines, demonstrating both N‐ GT and O ‐GT activity. GT72B1 showed little activity towards natural products with the exception of the tyrosine catabolite 4‐hydroxyphenylpyruvic acid. Both O‐ GT and N‐ GT activities were enhanced in both plants and cultures treated with herbicide safeners, demonstrating the chemical inducibility of this detoxification system in Arabidopsis .