Unknown

Dataset Information

0

A 13-lipoxygenase, TomloxC, is essential for synthesis of C5 flavour volatiles in tomato.


ABSTRACT: C5 volatile compounds, derived from fatty acids, are among the most important contributors to consumer liking of fresh tomatoes. Despite their important roles in flavour, the genes responsible for C5 volatile synthesis have yet to be identified. This work shows that their synthesis is catalysed in part by a 13-lipoxygenase (LOX), TomloxC, the same enzyme responsible for synthesis of C6 volatiles. C5 synthesis is independent of hydroperoxide lyase (HPL); moreover, HPL knockdown significantly increased C5 volatile synthesis. This LOX-dependent, HPL-independent pathway functions in both fruits and leaves. Synthesis of C5 volatiles increases in leaves following mechanical wounding but does not increase in response to infection with Xanthomonas campestris pv. vesicatoria. Large reductions in C5 and C6 volatiles in antisense TomloxC knockdown plants were observed but those reductions did not alter the development of disease symptoms, indicating that these volatiles do not have an important defensive function against this bacterial pathogen.

SUBMITTER: Shen J 

PROVIDER: S-EPMC3904703 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

A 13-lipoxygenase, TomloxC, is essential for synthesis of C5 flavour volatiles in tomato.

Shen Jiyuan J   Tieman Denise D   Jones Jeffrey B JB   Taylor Mark G MG   Schmelz Eric E   Huffaker Alisa A   Bies Dawn D   Chen Kunsong K   Klee Harry J HJ  

Journal of experimental botany 20140122 2


C5 volatile compounds, derived from fatty acids, are among the most important contributors to consumer liking of fresh tomatoes. Despite their important roles in flavour, the genes responsible for C5 volatile synthesis have yet to be identified. This work shows that their synthesis is catalysed in part by a 13-lipoxygenase (LOX), TomloxC, the same enzyme responsible for synthesis of C6 volatiles. C5 synthesis is independent of hydroperoxide lyase (HPL); moreover, HPL knockdown significantly incr  ...[more]

Similar Datasets

| S-EPMC6006436 | biostudies-literature
| S-EPMC4812756 | biostudies-literature
| S-EPMC4661238 | biostudies-literature
| S-EPMC1472464 | biostudies-literature
| S-EPMC5460189 | biostudies-literature
| S-EPMC8621488 | biostudies-literature
| S-EPMC2794349 | biostudies-literature
| S-EPMC3071775 | biostudies-literature
| S-EPMC10969657 | biostudies-literature
| S-EPMC8469758 | biostudies-literature