First published online March 20, 2003; 10.1104/pp.102.018572
Plant Physiol, April 2003, Vol. 131, pp. 1868-1876
Volatile Ester Formation in Roses. Identification of an
Acetyl-Coenzyme A. Geraniol/Citronellol Acetyltransferase in
Developing Rose Petals1
Moshe
Shalit,
Inna
Guterman,
Hanne
Volpin,
Einat
Bar,
Tal
Tamari,
Naama
Menda,
Zach
Adam,
Dani
Zamir,
Alexander
Vainstein,
David
Weiss,
Eran
Pichersky, and
Efraim
Lewinsohn*
Department of Vegetable Crops, Newe Ya'ar Research Center,
Agricultural Research Organization, P.O. Box 1021, Ramat Yishay 30095, Israel (M.S., E.B., T.T., E.L.); The Institute of Plant Sciences and
Genetics in Agriculture, Faculty of Agricultural, Food, and
Environmental Quality Sciences, The Hebrew University of Jerusalem,
P.O. Box 12, Rehovot 76100, Israel (M.S., I.G., N.M., Z.A., D.Z., A.V.,
D.W.); Department of Molecular, Cellular, and Developmental Biology,
University of Michigan, 830 North University Street, Ann Arbor,
Michigan 48109-1048 (E.P.); and Bioinformatics, Department of
Genomics, Agricultural Research Organization, Volcani Center, Bet Dagan
50250, Israel (H.V.)
The aroma of roses (Rosa hybrida) is due to
more than 400 volatile compounds including terpenes, esters, and
phenolic derivatives. 2-Phenylethyl acetate, cis-3-hexenyl
acetate, geranyl acetate, and citronellyl acetate were identified as
the main volatile esters emitted by the flowers of the scented rose
var. "Fragrant Cloud." Cell-free extracts of petals acetylated
several alcohols, utilizing acetyl-coenzyme A, to produce the
corresponding acetate esters. Screening for genes similar to known
plant alcohol acetyltransferases in a rose expressed sequence tag
database yielded a cDNA (RhAAT1) encoding a
protein with high similarity to several members of the BAHD
family of acyltransferases. This cDNA was functionally expressed in
Escherichia coli, and its gene product displayed acetyl-coenzyme A:geraniol acetyltransferase enzymatic activity in
vitro. The RhAAT1 protein accepted other alcohols such as citronellol and 1-octanol as substrates, but 2-phenylethyl alcohol and
cis-3-hexen-1-ol were poor substrates, suggesting that
additional acetyltransferases are present in rose petals. The RhAAT1
protein is a polypeptide of 458 amino acids, with a calculated
molecular mass of 51.8 kD, pI of 5.45, and is active as a monomer. The
RhAAT1 gene was expressed exclusively in floral tissue
with maximum transcript levels occurring at stage 4 of flower
development, where scent emission is at its peak.
1
This work was supported by the Israeli Ministry
of Sciences, Culture, and Sport (grant no. 1410-2-00 to E.L., D.Z.,
Z.A., A.V., and D.W.), and by a BARD scholarship (to E.P.).
This is publication no. 143/2002 of the Agricultural Research
Organization (Bet Dagan, Israel).
*
Corresponding author; e-mail twefraim{at}volcani.agri.gov.il;
fax 972-4-983-6936.
© 2003 American Society of Plant Biologists
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