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J Plant Physiol. 2017 Nov;218:35-44. doi: 10.1016/j.jplph.2017.07.013. Epub 2017 Jul 21.

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

Author information

1
Centro de Ciências do Mar, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: xanafilippe@gmail.com.
2
Centro de Ciências do Mar, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: jccardo@ualg.pt.
3
Centre for Mediterranean Bioresources and Food (MeditBio), Faculdade de Ciências e Tecnologia, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: mgmiguel@ualg.pt.
4
Centro de Ciências do Mar, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: lanjos@ualg.pt.
5
Centro de Estudos do Ambiente e do Mar Lisboa, Faculdade de Ciências, Universidade de Lisboa, CBV, DBV, 1749-016 Lisboa, Portugal. Electronic address: htrindade@fc.ul.pt.
6
Centro de Estudos do Ambiente e do Mar Lisboa, Faculdade de Ciências, Universidade de Lisboa, CBV, DBV, 1749-016 Lisboa, Portugal. Electronic address: acsf@fc.ul.pt.
7
Centro de Estudos do Ambiente e do Mar Lisboa, Faculdade de Ciências, Universidade de Lisboa, CBV, DBV, 1749-016 Lisboa, Portugal. Electronic address: jmbarroso@fc.ul.pt.
8
Centro de Ciências do Mar, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: dpower@ualg.pt.
9
Center of Electronics, Optoelectronics and Telecommunications, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. Electronic address: nmarques@ualg.pt.

Abstract

The 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 RRx8W 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 α-pinene, β-pinene, sabinene and β-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.

KEYWORDS:

1,8-cineole; Geranyl diphosphate; Heterologous expression; Terpene synthase; Thymus albicans

PMID:
28763707
DOI:
10.1016/j.jplph.2017.07.013
[Indexed for MEDLINE]

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