Two key polymorphisms in a newly discovered allele of the Vitis vinifera TPS24 gene are responsible for the production of the rotundone precursor α-guaiene

© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 67(2016), 3 vom: 15. Feb., Seite 799-808
1. Verfasser: Drew, Damian Paul (VerfasserIn)
Weitere Verfasser: Andersen, Trine Bundgaard, Sweetman, Crystal, Møller, Birger Lindberg, Ford, Christopher, Simonsen, Henrik Toft
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Pinot Noir Shiraz rotundone sesquiterpene synthase sesquiterpenoids wine aroma. Azulenes Plant Proteins mehr... Sesquiterpenes Sesquiterpenes, Guaiane Volatile Organic Compounds guaiene 88-84-6
Beschreibung
Zusammenfassung:© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Rotundone was initially identified as a grape-derived compound responsible for the peppery aroma of Shiraz wine varieties. It has subsequently been found in black and white pepper and several other spices. Because of its potent aroma, the molecular basis for rotundone formation is of particular relevance to grape and wine scientists and industry. We have identified and functionally characterized in planta a sesquiterpene synthase, VvGuaS, from developing grape berries, and have demonstrated that it produces the precursor of rotundone, α-guaiene, as its main product. The VvGuaS enzyme is a novel allele of the sesquiterpene synthase gene, VvTPS24, which has previously been reported to encode VvPNSeInt, an enzyme that produces a variety of selinene-type sesquiterpenes. This newly discovered VvTPS24 allele encodes an enzyme 99.5% identical to VvPNSeInt, with the differences comprising just 6 out of the 561 amino acid residues. Molecular modelling of the enzymes revealed that two of these residues, T414 and V530, are located in the active site of VvGuaS within 4 Å of the binding-site of the substrate, farnesyl pyrophosphate. Mutation of these two residues of VvGuaS into the corresponding polymorphisms in VvPNSeInt results in a complete functional conversion of one enzyme into the other, while mutation of each residue individually produces an intermediate change in the product profile. We have therefore demonstrated that VvGuaS, an enzyme responsible for production of the rotundone precursor, α-guaiene, is encoded by a novel allele of the previously characterized grapevine gene VvTPS24 and that two specific polymorphisms are responsible for functional differences between VvTPS24 alleles
Beschreibung:Date Completed 25.10.2016
Date Revised 24.03.2024
published: Print-Electronic
CommentIn: J Exp Bot. 2016 Feb;67(3):555-7. - PMID 26839218
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erv491