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Plant Physiol, September 2002, Vol. 130, pp. 466-476
Characterization of an Acyltransferase Capable of Synthesizing
Benzylbenzoate and Other Volatile Esters in Flowers and Damaged Leaves
of Clarkia breweri1
John C.
D'Auria,
Feng
Chen, and
Eran
Pichersky*
Department of Molecular, Cellular, and Developmental Biology,
University of Michigan, Ann Arbor, Michigan 48109-1048
A cDNA encoding a protein with 456 amino acids whose
sequence shows considerable similarity to plant acyltransferases was identified among 750 Clarkia breweri flower expressed
sequence tags. The cDNA was expressed in Escherichia
coli, and the protein produced was shown to encode the enzyme
benzoyl-coenzyme A (CoA):benzyl alcohol benzoyl transferase (BEBT).
BEBT catalyzes the formation of benzylbenzoate, a minor constituent of
the C. breweri floral aroma, but it also has activity
with a number of other alcohols and acyl CoAs. The BEBT
gene is expressed in different parts of the flowers with maximal RNA
transcript levels in the stigma, and no expression was observed in the
leaves under normal conditions. However, BEBT expression was induced in
damaged leaves, reaching a maximum 6 h after damage occurred. We
also show here that a closely related tobacco (Nicotiana
tabacum) gene previously shown to be induced in leaves after
being challenged by phytopathogenic bacteria also has BEBT activity,
whereas the most similar protein to BEBT in the Arabidopsis proteome
does not use benzoyl CoA as a substrate and instead can use acetyl CoA
to catalyze the formation of cis-3-hexen-1-yl acetate, a green-leaf volatile.
1
This work was supported by the National Science
Foundation (grant no. MCB-9974463), by Novartis Agribusiness
Biotechnology Research, Inc., and by a National Institutes of Health
training grant fellowship in genetics to J.C.D. (grant no. 5 T32 GM07544).
*
Corresponding author; e-mail: lelx{at}umich.edu; fax 734-647-0884.
© 2002 American Society of Plant Physiologists
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