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Originally published In Press as doi:10.1074/jbc.M107763200 on October 23, 2001
J. Biol. Chem., Vol. 277, Issue 1, 416-423, January 4, 2002
Lipoxygenase H1 Gene Silencing Reveals a Specific Role
in Supplying Fatty Acid Hydroperoxides for Aliphatic Aldehyde
Production*
José
León §,
Joaquín
Royo ¶,
Guy
Vancanneyt ,
Carlos
Sanz**,
Helena
Silkowski ,
Gareth
Griffiths , and
José J.
Sánchez-Serrano §§
From the Centro Nacional de Biotecnología,
Consejo Superior de Investigaciones Científicas, Campus de
Cantoblanco, Universidad Autónoma de Madrid Colmenar Viejo km
15,500, 28049 Madrid, Spain, the ** Instituto de la
Grasa, Consejo Superior de Investigaciones Científicas,
Avenida Padre García Tejero 4, 41012 Sevilla, Spain, and
 Horticulture Research International,
Wellesbourne, Warwick 35CV 9EF, United Kingdom
Lipoxygenases catalyze the formation
of fatty acid hydroperoxide precursors of an array of compounds
involved in the regulation of plant development and responses to
stress. To elucidate the function of the potato 13-lipoxygenase H1
(LOX H1), we have generated transgenic potato plants with reduced
expression of the LOX H1 gene as a consequence of
co-suppression-mediated gene silencing. Three independent LOX
H1-silenced transgenic lines were obtained, having less than 1%
of the LOX H1 protein present in wild-type plants. This depletion of
LOX H1 has no effect on the basal or wound-induced levels of jasmonates
derived from 13-hydroperoxylinolenic acid. However, LOX H1 depletion
results in a marked reduction in the production of volatile aliphatic
C6 aldehydes. These compounds are involved in plant defense responses,
acting as either signaling molecules for wound-induced gene expression
or as antimicrobial substances. LOX H1 protein was localized to the
chloroplast and the protein, expressed in Escherichia coli,
showed activity toward unesterified linoleic and linolenic acids and
plastidic phosphatidylglycerol. The results demonstrate that LOX H1 is
a specific isoform involved in the generation of volatile defense and
signaling compounds through the HPL branch of the octadecanoid pathway.
*
This work was supported by Spanish Comisión
Interministerial de Ciencia y Tecnología Grant BIO99-1225, by
Spanish Ministerio de Educación y Ciencia postdoctoral contracts
(to J. L. and J. R.) and postdoctoral fellowship (to G. V.), and by the Spanish Ministerio de Educación y Ciencia-British
Council Acciones Integradas Program (to J. J. S.-S. and
G. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
§
Present address: Inst. de Biologia Molecular y Celular de Plantas,
Universidad Politécnica de Valencia, Consejo Superior de
Investigaciones Científicas, 46022 Valencia, Spain.
¶
Present address: Dept. de Biología Celular y
Genética, Universidad de Alcalá de Henares, 28871 Madrid, Spain.
Present address: Aventis CropScience, B-9000 Ghent, Belgium.
§§
To whom correspondence should be addressed. Tel.: 34-91-5854500;
Fax: 34-91-5854506; E-mail: jjss@cnb.uam.es.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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