Hydroperoxide lyase depletion in transgenic potato plants leads to an increase in aphid performance.
Hydroperoxide lyases (HPLs) catalyze the cleavage of fatty acid hydroperoxides to aldehydes and oxoacids. These volatile aldehydes play a major role in forming the aroma of many plant fruits and flowers. In addition, they have antimicrobial activity in vitro and thus are thought to be involved in the plant defense response against pest and pathogen attack. An HPL activity present in potato leaves has been characterized and shown to cleave specifically 13-hydroperoxides of both linoleic and linolenic acids to yield hexanal and 3-hexenal, respectively, and 12-oxo-dodecenoic acid. A cDNA encoding this HPL has been isolated and used to monitor gene expression in healthy and mechanically damaged potato plants. HPL gene expression is subject to developmental control, being high in young leaves and attenuated in older ones, and it is induced weakly by wounding. HPL enzymatic activity, nevertheless, remains constant in leaves of different ages and also after wounding, suggesting that posttranscriptional mechanisms may regulate its activity levels. Antisense-mediated HPL depletion in transgenic potato plants has identified this enzyme as a major route of 13-fatty acid hydroperoxide degradation in the leaves. Although these transgenic plants have highly reduced levels of both hexanal and 3-hexenal, they show no phenotypic differences compared with wild-type ones, particularly in regard to the expression of wound-induced genes. However, aphids feeding on the HPL-depleted plants display approximately a two-fold increase in fecundity above those feeding on nontransformed plants, consistent with the hypothesis that HPL-derived products have a negative impact on aphid performance. Thus, HPL-catalyzed production of C6 aldehydes may be a key step of a built-in resistance mechanism of plants against some sucking insect pests.
Vancanneyt
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G
Departamento de Genética Molecular de Plantas, Centro Nacional de Biotecnologia, Consejo Superior de Investigaciones Cientificas, Campus de Cantoblanco Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Sanz
C
C
Farmaki
T
T
Paneque
M
M
Ortego
F
F
Castañera
P
P
Sánchez-Serrano
J J
JJ
D000446:Aldehyde-Lyases / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D000818:Animals; D001042:Aphids; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D018506:Gene Expression Regulation, Plant / Q000276:immunology; D008969:Molecular Sequence Data; D010935:Plant Diseases; D030821:Plants, Genetically Modified; D011198:Solanum tuberosum / Q000235:genetics* / Q000276:immunology / Q000378:metabolism
D003577:Cytochrome P-450 Enzyme System; D000446:Aldehyde-Lyases; C054540:hydroperoxide lyase