MycorrhizaeV1, Main, Corpus, bibRecord, 002873

Role of carotenoid cleavage dioxygenase 1 (CCD1) in apocarotenoid biogenesis revisited.

Identifieur interne : 002873 ( Main/Corpus ); précédent : 002872; suivant : 002874

Role of carotenoid cleavage dioxygenase 1 (CCD1) in apocarotenoid biogenesis revisited.

Auteurs : Daniela S. Floss ; Michael H. Walter

Source :

Plant signaling & behavior [ 1559-2324 ] ; 2009.

RBID : pubmed:19721743

English descriptors

KwdEn :
- Carotenoids (biosynthesis), Dioxygenases (metabolism), Medicago truncatula (enzymology), Mycorrhizae (MeSH), Plant Roots (enzymology), Substrate Specificity (MeSH).
MESH :
- chemical , biosynthesis : Carotenoids.
- chemical , metabolism : Dioxygenases.
- enzymology : Medicago truncatula, Plant Roots.
- Mycorrhizae, Substrate Specificity.

Abstract

Oxidative tailoring of C(40) carotenoids by double bond-specific cleavage enzymes (carotenoid cleavage dioxygenases, CCDs) gives rise to various apocarotenoids. AtCCD1 generating C(13) and C(14) apocarotenoids and orthologous enzymes in other plants are the only CCDs acting in the cytosol, while the hitherto presumed C(40) substrate is localized in the plastid. A new model for CCD1 action arising from a RNAi-mediated CCD1 gene silencing study in mycorrhizal hairy roots of Medicago truncatula may solve this contradiction. This approach unexpectedly resulted in the accumulation of C(27) apocarotenoids but not C(40) carotenoids suggesting C(27) as the main substrates for CCD1 in planta. It further implies a consecutive two-step cleavage process, in which another CCD performs the primary cleavage of C(40) to C(27) in the plastid followed by C(27) export and further cleavage by CCD1 in the cytosol. We compare the specificities and subcellular locations of the various CCDs and propose the plastidial CCD7 to be the first player in mycorrhizal apocarotenoid biogenesis.

DOI: 10.4161/psb.4.3.7840
PubMed: 19721743
PubMed Central: PMC2652522

Links to Exploration step

pubmed:19721743

Le document en format XML

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<author><name sortKey="Floss, Daniela S" sort="Floss, Daniela S" uniqKey="Floss D" first="Daniela S" last="Floss">Daniela S. Floss</name>
<affiliation><nlm:affiliation>Leibniz-Institut für Pflanzenbiochemie (IPB), Abteilung Sekundärstoffwechsel, Halle (Saale), Germany.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Walter, Michael H" sort="Walter, Michael H" uniqKey="Walter M" first="Michael H" last="Walter">Michael H. Walter</name>
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<affiliation><nlm:affiliation>Leibniz-Institut für Pflanzenbiochemie (IPB), Abteilung Sekundärstoffwechsel, Halle (Saale), Germany.</nlm:affiliation>
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<author><name sortKey="Walter, Michael H" sort="Walter, Michael H" uniqKey="Walter M" first="Michael H" last="Walter">Michael H. Walter</name>
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<series><title level="j">Plant signaling & behavior</title>
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<term>Dioxygenases (metabolism)</term>
<term>Medicago truncatula (enzymology)</term>
<term>Mycorrhizae (MeSH)</term>
<term>Plant Roots (enzymology)</term>
<term>Substrate Specificity (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Oxidative tailoring of C(40) carotenoids by double bond-specific cleavage enzymes (carotenoid cleavage dioxygenases, CCDs) gives rise to various apocarotenoids. AtCCD1 generating C(13) and C(14) apocarotenoids and orthologous enzymes in other plants are the only CCDs acting in the cytosol, while the hitherto presumed C(40) substrate is localized in the plastid. A new model for CCD1 action arising from a RNAi-mediated CCD1 gene silencing study in mycorrhizal hairy roots of Medicago truncatula may solve this contradiction. This approach unexpectedly resulted in the accumulation of C(27) apocarotenoids but not C(40) carotenoids suggesting C(27) as the main substrates for CCD1 in planta. It further implies a consecutive two-step cleavage process, in which another CCD performs the primary cleavage of C(40) to C(27) in the plastid followed by C(27) export and further cleavage by CCD1 in the cytosol. We compare the specificities and subcellular locations of the various CCDs and propose the plastidial CCD7 to be the first player in mycorrhizal apocarotenoid biogenesis.</div>
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<Month>10</Month>
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<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>16</Day>
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<JournalIssue CitedMedium="Internet"><Volume>4</Volume>
<Issue>3</Issue>
<PubDate><Year>2009</Year>
<Month>Mar</Month>
</PubDate>
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<Title>Plant signaling & behavior</Title>
<ISOAbbreviation>Plant Signal Behav</ISOAbbreviation>
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<ArticleTitle>Role of carotenoid cleavage dioxygenase 1 (CCD1) in apocarotenoid biogenesis revisited.</ArticleTitle>
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<Abstract><AbstractText>Oxidative tailoring of C(40) carotenoids by double bond-specific cleavage enzymes (carotenoid cleavage dioxygenases, CCDs) gives rise to various apocarotenoids. AtCCD1 generating C(13) and C(14) apocarotenoids and orthologous enzymes in other plants are the only CCDs acting in the cytosol, while the hitherto presumed C(40) substrate is localized in the plastid. A new model for CCD1 action arising from a RNAi-mediated CCD1 gene silencing study in mycorrhizal hairy roots of Medicago truncatula may solve this contradiction. This approach unexpectedly resulted in the accumulation of C(27) apocarotenoids but not C(40) carotenoids suggesting C(27) as the main substrates for CCD1 in planta. It further implies a consecutive two-step cleavage process, in which another CCD performs the primary cleavage of C(40) to C(27) in the plastid followed by C(27) export and further cleavage by CCD1 in the cytosol. We compare the specificities and subcellular locations of the various CCDs and propose the plastidial CCD7 to be the first player in mycorrhizal apocarotenoid biogenesis.</AbstractText>
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<ForeName>Daniela S</ForeName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">C13 apocarotenoids</Keyword>
<Keyword MajorTopicYN="N">abscisic acid</Keyword>
<Keyword MajorTopicYN="N">arbuscular mycorrhiza</Keyword>
<Keyword MajorTopicYN="N">aroma compounds</Keyword>
<Keyword MajorTopicYN="N">carotenoid cleavage dioxygenase CCD1</Keyword>
<Keyword MajorTopicYN="N">norisoprenoids</Keyword>
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Role of carotenoid cleavage dioxygenase 1 (CCD1) in apocarotenoid biogenesis revisited.

Role of carotenoid cleavage dioxygenase 1 (CCD1) in apocarotenoid biogenesis revisited.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki