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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- -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--Glcs to generate
1,2-di-O-acyl--Glc and anomeric acyl exchange between
1-O-acyl--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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