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Molecular cloning and functional characterization of a monoterpene synthase isolated from the aromatic wild shrub Thymus albicans

2017-11Journal article Open access
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dc.contributor.authorFilipe, Alexandra
dc.contributor.authorCardoso, João
dc.contributor.authorMiguel, Maria Graca
dc.contributor.authorAnjos, Liliana
dc.contributor.authorTrindade, Helena
dc.contributor.authorFigueiredo, Ana Cristina
dc.contributor.authorBarroso, Jose
dc.contributor.authorPower, Deborah
dc.contributor.authorMarques, N T.
dc.date.accessioned2019-11-20T15:07:15Z
dc.date.available2020-11-01T01:30:13Z
dc.date.issued2017-11
dc.description.abstractThe essential oil of Thymus albicans Hoffmanns. & Link, a native shrub from the Iberian Peninsula, is mainly composed of monoterpenes. In this study, a 1,8-cineole synthase was isolated from the 1,8-cineole chemotype. A partial sequence that lacked the complete plastid transit peptide but contained an extended C-terminal when compared to other related terpene synthases was generated by PCR and Rapid Amplification of cDNA Ends (RACE). The predicted mature polypeptide was 593 amino acids in length and shared 78% and 77% sequence similarity with the homologue 1,8-cineole synthase from Rosmarinus officinalis and Salvia officinalis, respectively. The putative protein possessed the characteristic conserved motifs of plant monoterpene synthases including the RRx(8)W and DDxxD motifs and phylogenetic analysis indicated that the amplified 1,8-cineole synthase bears greater sequence similarity with other 1,8-cineole synthases from Lamiaceae family relative to the terpene synthases from the genus Thymus. Functional expression of the recombinant protein in Escherichia coli revealed that in the presence of geranyl diphosphate (GPP) 1,8-cineole was the major product but that its production was too low for robust quantification. Other minor conversion products included a-pinene, beta-pinene, sabinene and beta-myrcene suggesting the isolated 1,8-cineole synthase may be a multi-product enzyme. To our knowledge, this is the first report of a functionally characterized monoterpene synthase from Thymus albicans.
dc.description.sponsorshipCeratonia Project MONOTHYMUS, Universidade do Algarve, Portugal
dc.description.sponsorshipMinistry of Science, Portugal
dc.description.sponsorshipFCT under FEDER PT2020-Compete
dc.description.sponsorship[FCT/UID/Multi/00631/2013/CEOT]
dc.identifier.doi10.1016/j.jplph.2017.07.013
dc.identifier.issn0176-1617
dc.identifier.issn1618-1328
dc.identifier.urihttp://hdl.handle.net/10400.1/12945
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier Gmbh, Urban & Fischer Verlag
dc.subjectEssential oils
dc.subjectTerpene synthases
dc.subjectPhylogenetic analysis
dc.subjectGenomic organization
dc.subjectEscherichia-coli
dc.subjectCdna isolation
dc.subjectExpression
dc.subjectProtein
dc.subjectCaespititius
dc.subjectMastichina
dc.titleMolecular cloning and functional characterization of a monoterpene synthase isolated from the aromatic wild shrub Thymus albicans
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F79105%2F2011/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FAMB%2F50017%2F2013/PT
oaire.citation.endPage44
oaire.citation.startPage35
oaire.citation.titleJournal of Plant Physiology
oaire.citation.volume218
oaire.fundingStreamSFRH
oaire.fundingStream5876
person.familyNameCardoso
person.familyNameMiguel
person.familyNameAnjos Guerreiro
person.familyNamePower
person.familyNameTomás Marques
person.givenNameJoão
person.givenNameMaria
person.givenNameLiliana Isabel Tomé
person.givenNameDeborah Mary
person.givenNameNatália
person.identifier14332
person.identifierAAK-3800-2020
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person.identifier.orcid0000-0001-9474-522X
person.identifier.orcid0000-0003-1366-0246
person.identifier.orcid0000-0002-0222-621X
person.identifier.ridM-4151-2013
person.identifier.scopus-author-id7201822956
person.identifier.scopus-author-id9941792100
person.identifier.scopus-author-id8575757700
person.identifier.scopus-author-id7101806760
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticle
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