The Oxygenase CAO-1 of Neurospora crassa Is a Resveratrol Cleavage Enzyme

Handle URI:
http://hdl.handle.net/10754/554122
Title:
The Oxygenase CAO-1 of Neurospora crassa Is a Resveratrol Cleavage Enzyme
Authors:
Diaz-Sanchez, V.; F. Estrada, A.; Limon, M. C.; Al-Babili, Salim ( 0000-0003-4823-2882 ) ; Avalos, J.
Abstract:
The genome of the ascomycete Neurospora crassa encodes CAO-1 and CAO-2, two members of the carotenoid cleavage oxygenase family that target double bonds in different substrates. Previous studies demonstrated the role of CAO-2 in cleaving the C40 carotene torulene, a key step in the synthesis of the C35 apocarotenoid pigment neurosporaxanthin. In this work, we investigated the activity of CAO-1, assuming that it may provide retinal, the chromophore of the NOP-1 rhodopsin, by cleaving β-carotene. For this purpose, we tested CAO-1 activity with carotenoid substrates that were, however, not converted. In contrast and consistent with its sequence similarity to family members that act on stilbenes, CAO-1 cleaved the interphenyl Cα-Cβ double bond of resveratrol and its derivative piceatannol. CAO-1 did not convert five other similar stilbenes, indicating a requirement for a minimal number of unmodified hydroxyl groups in the stilbene background. Confirming its biological function in converting stilbenes, adding resveratrol led to a pronounced increase in cao-1 mRNA levels, while light, a key regulator of carotenoid metabolism, did not alter them. Targeted Δcao-1 mutants were not impaired by the presence of resveratrol, a phytoalexin active against different fungi, which did not significantly affect the growth and development of wild-type Neurospora. However, under partial sorbose toxicity, the Δcao-1 colonies exhibited faster radial growth than control strains in the presence of resveratrol, suggesting a moderate toxic effect of resveratrol cleavage products.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
The Oxygenase CAO-1 of Neurospora crassa Is a Resveratrol Cleavage Enzyme 2013, 12 (9):1305 Eukaryotic Cell
Journal:
Eukaryotic Cell
Issue Date:
26-Jul-2013
DOI:
10.1128/EC.00084-13
PubMed ID:
23893079
PubMed Central ID:
PMC3811574
Type:
Article
ISSN:
1535-9778; 1535-9786
Additional Links:
http://ec.asm.org/cgi/doi/10.1128/EC.00084-13
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorDiaz-Sanchez, V.en
dc.contributor.authorF. Estrada, A.en
dc.contributor.authorLimon, M. C.en
dc.contributor.authorAl-Babili, Salimen
dc.contributor.authorAvalos, J.en
dc.date.accessioned2015-05-18T21:54:41Zen
dc.date.available2015-05-18T21:54:41Zen
dc.date.issued2013-07-26en
dc.identifier.citationThe Oxygenase CAO-1 of Neurospora crassa Is a Resveratrol Cleavage Enzyme 2013, 12 (9):1305 Eukaryotic Cellen
dc.identifier.issn1535-9778en
dc.identifier.issn1535-9786en
dc.identifier.pmid23893079en
dc.identifier.doi10.1128/EC.00084-13en
dc.identifier.urihttp://hdl.handle.net/10754/554122en
dc.description.abstractThe genome of the ascomycete Neurospora crassa encodes CAO-1 and CAO-2, two members of the carotenoid cleavage oxygenase family that target double bonds in different substrates. Previous studies demonstrated the role of CAO-2 in cleaving the C40 carotene torulene, a key step in the synthesis of the C35 apocarotenoid pigment neurosporaxanthin. In this work, we investigated the activity of CAO-1, assuming that it may provide retinal, the chromophore of the NOP-1 rhodopsin, by cleaving β-carotene. For this purpose, we tested CAO-1 activity with carotenoid substrates that were, however, not converted. In contrast and consistent with its sequence similarity to family members that act on stilbenes, CAO-1 cleaved the interphenyl Cα-Cβ double bond of resveratrol and its derivative piceatannol. CAO-1 did not convert five other similar stilbenes, indicating a requirement for a minimal number of unmodified hydroxyl groups in the stilbene background. Confirming its biological function in converting stilbenes, adding resveratrol led to a pronounced increase in cao-1 mRNA levels, while light, a key regulator of carotenoid metabolism, did not alter them. Targeted Δcao-1 mutants were not impaired by the presence of resveratrol, a phytoalexin active against different fungi, which did not significantly affect the growth and development of wild-type Neurospora. However, under partial sorbose toxicity, the Δcao-1 colonies exhibited faster radial growth than control strains in the presence of resveratrol, suggesting a moderate toxic effect of resveratrol cleavage products.en
dc.relation.urlhttp://ec.asm.org/cgi/doi/10.1128/EC.00084-13en
dc.rightsArchived with thanks to Eukaryotic Cellen
dc.titleThe Oxygenase CAO-1 of Neurospora crassa Is a Resveratrol Cleavage Enzymeen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalEukaryotic Cellen
dc.identifier.pmcidPMC3811574en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDepartamento de Genética, Universidad de Sevilla, Seville, Spainen
dc.contributor.institutionFaculty of Biology, Albert-Ludwigs University of Freiburg, Freiburg, Germanyen
kaust.authorAl-Babili, Salimen

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