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Plant Physiol, October 1999, Vol. 121, pp. 453-460

Glucose Polyester Biosynthesis. Purification and Characterization of a Glucose Acyltransferase1

Alice X. Li,2 Nancy Eannetta, Gurdev S. Ghangas, and John C. Steffens3*

Department of Plant Breeding, Cornell University, Ithaca, New York 14853

Glandular trichomes of the wild tomato species Lycopersicon pennellii secrete 2,3,4-O-tri-acyl-glucose (-Glc), which contributes to insect resistance. A Glc acyltransferase catalyzes the formation of diacyl-Glc by disproportionating two equivalents of 1-O-acyl-beta -Glc, a high-energy molecule formed by a UDP-Glc dependent reaction. The acyltransferase was purified 4,900-fold from L. pennellii leaves by polyethylene glycol fractionation, diethylaminoethyl chromatography, concanavalin A affinity chromatography, and chromatofocusing. The acyltransferase possesses an isoelectric point of 4.8, a relative molecular mass around 110 kD, and is composed of 34- and 24-kD polypeptides as a heterotetramer. The 34- and 24-kD proteins were partially sequenced. The purified enzyme catalyzes both the disproportionation of 1-O-acyl-beta -Glcs to generate 1,2-di-O-acyl-beta -Glc and anomeric acyl exchange between 1-O-acyl-beta -Glc and Glc.

1 This work was supported by the Cornell Center for Advanced Technology in Biotechnology, which is sponsored by the New York State Science and Technology Foundation and by industrial partners, and by Hatch Project no. 149,417.

2 Present address: BioArray Solutions, 120 Centennial Avenue, Piscataway, NJ 08854.

3 Present address: Novartis Agribusiness Biotechnology Research, Inc., 3054 Cornwallis Road, Research Triangle Park, NC 27709.

* Corresponding author; e-mail john.steffens{at}nabri.novartis.com;fax 919-541-8585.

© 1999 American Society of Plant Physiologists


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