PoplarV1, Main, Exploration, bibRecord, 002039

Stress-responsive hydroxycinnamate glycosyltransferase modulates phenylpropanoid metabolism in Populus.

Identifieur interne : 002039 ( Main/Exploration ); précédent : 002038; suivant : 002040

Stress-responsive hydroxycinnamate glycosyltransferase modulates phenylpropanoid metabolism in Populus.

Auteurs : Benjamin A. Babst [États-Unis] ; Han-Yi Chen [États-Unis] ; Hong-Qiang Wang [États-Unis] ; Raja S. Payyavula [États-Unis] ; Tina P. Thomas [États-Unis] ; Scott A. Harding [États-Unis] ; Chung-Jui Tsai [États-Unis]

Source :

Journal of experimental botany [ 1460-2431 ] ; 2014.

RBID : pubmed:24803501

Descripteurs français

KwdFr :
- Acides coumariques (métabolisme), Famille multigénique (MeSH), Glycosyltransferase (métabolisme), Hydroxybenzoates (métabolisme), Phylogenèse (MeSH), Populus (enzymologie), Populus (génétique), Protéines végétales (génétique), Protéines végétales (métabolisme), Stress physiologique (MeSH), Végétaux génétiquement modifiés (MeSH).
MESH :
- enzymologie : Populus.
- génétique : Populus, Protéines végétales.
- métabolisme : Acides coumariques, Glycosyltransferase, Hydroxybenzoates, Protéines végétales.
- Famille multigénique, Phylogenèse, Stress physiologique, Végétaux génétiquement modifiés.

English descriptors

KwdEn :
- Coumaric Acids (metabolism), Glycosyltransferases (metabolism), Hydroxybenzoates (metabolism), Multigene Family (MeSH), Phylogeny (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Plants, Genetically Modified (MeSH), Populus (enzymology), Populus (genetics), Stress, Physiological (MeSH).
MESH :
- chemical , genetics : Plant Proteins.
- chemical , metabolism : Coumaric Acids, Glycosyltransferases, Hydroxybenzoates, Plant Proteins.
- enzymology : Populus.
- genetics : Populus.
- Multigene Family, Phylogeny, Plants, Genetically Modified, Stress, Physiological.

Abstract

The diversity of phenylpropanoids offers a rich inventory of bioactive chemicals that can be exploited for plant improvement and human health. Recent evidence suggests that glycosylation may play a role in the partitioning of phenylpropanoid precursors for a variety of downstream uses. This work reports the functional characterization of a stress-responsive glycosyltransferase, GT1-316 in Populus. GT1-316 belongs to the UGT84A subfamily of plant glycosyltransferase family 1 and is designated UGT84A17. Recombinant protein analysis showed that UGT84A17 is a hydroxycinnamate glycosyltransferase and able to accept a range of unsubstituted and substituted cinnamic and benzoic acids as substrates in vitro. Overexpression of GT1-316 in transgenic Populus led to plant-wide increases of hydroxycinnamoyl-glucose esters, which were further elevated under N-limiting conditions. Levels of the two most abundant flavonoid glycosides, rutin and kaempferol-3-O-rutinoside, decreased, while levels of other less abundant flavonoid and phenylpropanoid conjugates increased in leaves of the GT1-316-overexpressing plants. Transcript levels of representative phenylpropanoid pathway genes were unchanged in transgenic plants, supporting a glycosylation-mediated redirection of phenylpropanoid carbon flow as opposed to enhanced phenylpropanoid pathway flux. The metabolic response of N-replete transgenic plants overlapped with that of N-stressed wild types, as the majority of phenylpropanoid derivatives significantly affected by GT1-316 overexpression were also significantly changed by N stress in the wild types. These results suggest that UGT84A17 plays an important role in phenylpropanoid metabolism by modulating biosynthesis of hydroxycinnamoyl-glucose esters and their derivatives in response to developmental and environmental cues.

DOI: 10.1093/jxb/eru192
PubMed: 24803501
PubMed Central: PMC4112628

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 002197
to stream Main, to step Curation: 002197

Le document en format XML

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<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
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<front><div type="abstract" xml:lang="en">The diversity of phenylpropanoids offers a rich inventory of bioactive chemicals that can be exploited for plant improvement and human health. Recent evidence suggests that glycosylation may play a role in the partitioning of phenylpropanoid precursors for a variety of downstream uses. This work reports the functional characterization of a stress-responsive glycosyltransferase, GT1-316 in Populus. GT1-316 belongs to the UGT84A subfamily of plant glycosyltransferase family 1 and is designated UGT84A17. Recombinant protein analysis showed that UGT84A17 is a hydroxycinnamate glycosyltransferase and able to accept a range of unsubstituted and substituted cinnamic and benzoic acids as substrates in vitro. Overexpression of GT1-316 in transgenic Populus led to plant-wide increases of hydroxycinnamoyl-glucose esters, which were further elevated under N-limiting conditions. Levels of the two most abundant flavonoid glycosides, rutin and kaempferol-3-O-rutinoside, decreased, while levels of other less abundant flavonoid and phenylpropanoid conjugates increased in leaves of the GT1-316-overexpressing plants. Transcript levels of representative phenylpropanoid pathway genes were unchanged in transgenic plants, supporting a glycosylation-mediated redirection of phenylpropanoid carbon flow as opposed to enhanced phenylpropanoid pathway flux. The metabolic response of N-replete transgenic plants overlapped with that of N-stressed wild types, as the majority of phenylpropanoid derivatives significantly affected by GT1-316 overexpression were also significantly changed by N stress in the wild types. These results suggest that UGT84A17 plays an important role in phenylpropanoid metabolism by modulating biosynthesis of hydroxycinnamoyl-glucose esters and their derivatives in response to developmental and environmental cues. </div>
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<Abstract><AbstractText>The diversity of phenylpropanoids offers a rich inventory of bioactive chemicals that can be exploited for plant improvement and human health. Recent evidence suggests that glycosylation may play a role in the partitioning of phenylpropanoid precursors for a variety of downstream uses. This work reports the functional characterization of a stress-responsive glycosyltransferase, GT1-316 in Populus. GT1-316 belongs to the UGT84A subfamily of plant glycosyltransferase family 1 and is designated UGT84A17. Recombinant protein analysis showed that UGT84A17 is a hydroxycinnamate glycosyltransferase and able to accept a range of unsubstituted and substituted cinnamic and benzoic acids as substrates in vitro. Overexpression of GT1-316 in transgenic Populus led to plant-wide increases of hydroxycinnamoyl-glucose esters, which were further elevated under N-limiting conditions. Levels of the two most abundant flavonoid glycosides, rutin and kaempferol-3-O-rutinoside, decreased, while levels of other less abundant flavonoid and phenylpropanoid conjugates increased in leaves of the GT1-316-overexpressing plants. Transcript levels of representative phenylpropanoid pathway genes were unchanged in transgenic plants, supporting a glycosylation-mediated redirection of phenylpropanoid carbon flow as opposed to enhanced phenylpropanoid pathway flux. The metabolic response of N-replete transgenic plants overlapped with that of N-stressed wild types, as the majority of phenylpropanoid derivatives significantly affected by GT1-316 overexpression were also significantly changed by N stress in the wild types. These results suggest that UGT84A17 plays an important role in phenylpropanoid metabolism by modulating biosynthesis of hydroxycinnamoyl-glucose esters and their derivatives in response to developmental and environmental cues. </AbstractText>
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Stress-responsive hydroxycinnamate glycosyltransferase modulates phenylpropanoid metabolism in Populus.

Stress-responsive hydroxycinnamate glycosyltransferase modulates phenylpropanoid metabolism in Populus.

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