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Plant Physiol, August 2000, Vol. 123, pp. 1561-1570
AN9, a Petunia Glutathione S-Transferase Required
for Anthocyanin Sequestration, Is a Flavonoid-Binding
Protein1
Lukas A.
Mueller,*
Christopher D.
Goodman,
Rebecca A.
Silady, and
Virginia
Walbot
Department of Biological Sciences, 385 Serra Mall, Stanford
University, Stanford, California 94305-5020
AN9 is a glutathione S-transferase from petunia
(Petunia hybrida) required for efficient anthocyanin
export from the site of synthesis in the cytoplasm into permanent
storage in the vacuole. For many xenobiotics it is well established
that a covalent glutathione (GSH) tag mediates recognition of molecules
destined for vacuolar sequestration by a tonoplast-localized
ATP-binding cassette pump. Here we inquired whether AN9 catalyzes the
formation of GSH conjugates with flavonoid substrates. Using
high-performance liquid chromatography analysis of reaction mixtures
containing enzyme, GSH, and flavonoids, including anthocyanins, we
could detect neither conjugates nor a decrease in the free thiol
concentration. These results suggest that no conjugate is formed in
vitro. However, AN9 was shown to bind flavonoids using three assays:
inhibition of the glutathione S-transferase activity of
AN9 toward the common substrate 1-chloro 2,4-dinitrobenzene,
equilibrium dialysis, and tryptophan quenching. We conclude that AN9 is
a flavonoid-binding protein, and propose that in vivo it serves as a
cytoplasmic flavonoid carrier protein.
1
This work was supported by the National Science
Foundation (grant no. IBN 9603927). L.A.M. was supported in part by a
postdoctoral fellowship from the Swiss National Science Foundation and
by a gift from the Educational Aid Program of the DuPont Company.
C.D.G. was supported in part by a Natural Sciences and Engineering
Research Council of Canada predoctoral fellowship.
*
Corresponding author; e-mail Lukas_Mueller{at}mail.com; fax
650-725-8221.
© 2000 American Society of Plant Physiologists
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