First published online April 9, 2002; 10.1104/pp.010747
Plant Physiol, May 2002, Vol. 129, pp. 321-332
Isolation and Characterization of Homogentisate Phytyltransferase
Genes from Synechocystis sp. PCC 6803 and
Arabidopsis
Beth
Savidge,
James D.
Weiss,
Yun-Hua H.
Wong,
Michael W.
Lassner,1
Timothy A.
Mitsky,
Christine K.
Shewmaker,
Dusty
Post-Beittenmiller, and
Henry E.
Valentin*
Monsanto Company, Calgene Campus, 1920 Fifth Street, Davis,
California 95616 (B.S., M.W.L., C.K.S.); and Monsanto Company, 800 N. Lindbergh Boulevard, St. Louis, Missouri 63167 (J.D.W.,
Y.-H.H.W., T.A.M., D.P.-B., H.E.V.)
Tocopherols, synthesized by photosynthetic organisms, are
micronutrients with antioxidant properties that play important roles in
animal and human nutrition. Because of these health benefits, there is
considerable interest in identifying the genes involved in tocopherol
biosynthesis to allow transgenic alteration of both tocopherol levels
and composition in agricultural crops. Tocopherols are generated from
the condensation of phytyldiphosphate and homogentisic acid (HGA),
followed by cyclization and methylation reactions. Homogentisate
phytyltransferase (HPT) performs the first committed step in this
pathway, the phytylation of HGA. In this study, bioinformatics techniques were used to identify candidate genes,
slr1736 and HPT1, that encode HPT from
Synechocystis sp. PCC 6803 and Arabidopsis, respectively. These two genes encode putative membrane-bound proteins, and contain amino acid residues highly conserved with other
prenyltransferases of the aromatic type. A Synechocystis
sp. PCC 6803 slr1736 null mutant obtained by
insertional inactivation did not accumulate tocopherols, and was
rescued by the Arabidopsis HPT1 ortholog. The membrane
fraction of wild-type Synechocystis sp. PCC 6803 was
capable of catalyzing the phytylation of HGA, whereas the membrane
fraction from the slr1736 null mutant was not. The
microsomal membrane fraction of baculovirus-infected insect cells
expressing the Synechocystis sp. PCC 6803 slr1736 were also able to perform the phytylation
reaction, verifying HPT activity of the protein encoded by this gene.
In addition, evidence that antisense expression of HPT1
in Arabidopsis resulted in reduced seed tocopherol levels, whereas
seed-specific sense expression resulted in increased seed tocopherol
levels, is presented.
1
Present address: Maxygen, Inc., 515 Galveston Drive, Redwood City, CA 94063.
*
Corresponding author; e-mail henry.e.valentin{at}monsanto.com;
fax 314-694-8275.
© 2002 American Society of Plant Physiologists
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