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Plant Physiol, February 2001, Vol. 125, pp. 847-855
Identification and Analysis of a Gene from Calendula
officinalis Encoding a Fatty Acid Conjugase
Xiao
Qiu,1*
Darwin W.
Reed,
Haiping
Hong,1
Samuel L.
MacKenzie, and
Patrick S.
Covello
Research and Development, Bioriginal Food and Science Corporation,
102 Melville Street, Saskatoon, Saskatchewan, Canada S7J 0R1 (X.Q.,
H.H.); and National Research Council of Canada, Plant Biotechnology
Institute, 110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N 0W9
(D.W.R., S.L.M., P.S.C.)
Two homologous cDNAs, CoFad2 and
CoFac2, were isolated from a Calendula
officinalis developing seed by a polymerase chain reaction-based cloning strategy. Both sequences share similarity to
FAD2 desaturases and FAD2-related enzymes. In C.
officinalis plants CoFad2 was expressed in all
tissues tested, whereas CoFac2 expression was specific
to developing seeds. Expression of CoFad2 cDNA in yeast
(Saccharomyces cerevisiae) indicated it encodes a  12
desaturase that introduces a double bond at the 12 position of
16:1(9Z) and 18:1(9Z). Expression of
CoFac2 in yeast revealed that the encoded enzyme acts as
a fatty acid conjugase converting 18:2(9Z,
12Z) to calendic acid 18:3(8E,
10E, 12Z). The enzyme also has weak
activity on the mono-unsaturates 16:1(9Z) and
18:1(9Z) producing compounds with the properties of 8,10 conjugated dienes.
1
Present address: National Research Council of
Canada, Plant Biotechnology Institute, 110 Gymnasium Place, Saskatoon,
SK, Canada S7N 0W9.
*
Corresponding author; e-mail xqiu{at}pbi.nrc.ca; fax
306-975-4839.
© 2001 American Society of Plant Physiologists
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