Characterization of Biosynthetic Pathways for the Production of the Volatile Homoterpenes DMNT and TMTT in Zea mays . Issue 10 (23rd September 2016)
- Record Type:
- Journal Article
- Title:
- Characterization of Biosynthetic Pathways for the Production of the Volatile Homoterpenes DMNT and TMTT in Zea mays . Issue 10 (23rd September 2016)
- Main Title:
- Characterization of Biosynthetic Pathways for the Production of the Volatile Homoterpenes DMNT and TMTT in Zea mays
- Authors:
- Richter, Annett
Schaff, Claudia
Zhang, Zhiwu
Lipka, Alexander E.
Tian, Feng
Köllner, Tobias G.
Schnee, Christiane
Preiß, Susanne
Irmisch, Sandra
Jander, Georg
Boland, Willhelm
Gershenzon, Jonathan
Buckler, Edward S.
Degenhardt, Jörg - Abstract:
- Abstract : Biosynthetic pathways for the terpenes DMNT and TMTT in maize ( Zea mays ) and their corresponding enzymes were identified by nested association mapping of herbivore-induced volatile terpenes. Abstract: Plant volatiles not only have multiple defense functions against herbivores, fungi, and bacteria, but also have been implicated in signaling within the plant and toward other organisms. Elucidating the function of individual plant volatiles will require more knowledge of their biosynthesis and regulation in response to external stimuli. By exploiting the variation of herbivore-induced volatiles among 26 maize ( Zea mays ) inbred lines, we conducted a nested association mapping and genome-wide association study (GWAS ) to identify a set of quantitative trait loci (QTLs) for investigating the pathways of volatile terpene production. The most significant identified QTL affects the emission of ( E )-nerolidol, linalool, and the two homoterpenes ( E )-3, 8-dimethyl-1, 4, 7-nonatriene (DMNT ) and ( E, E )-4, 8, 12-trimethyltrideca-1, 3, 7, 11-tetraene (TMTT ). GWAS associated a single nucleotide polymorphism in the promoter of the gene encoding the terpene synthase TPS2 with this QTL . Biochemical characterization of TPS2 verified that this plastid-localized enzyme forms linalool, ( E )-nerolidol, and ( E, E )-geranyllinalool. The subsequent conversion of ( E )-nerolidol into DMNT maps to a P450 monooxygenase, CYP92C5, which is capable of converting nerolidol into DMNTAbstract : Biosynthetic pathways for the terpenes DMNT and TMTT in maize ( Zea mays ) and their corresponding enzymes were identified by nested association mapping of herbivore-induced volatile terpenes. Abstract: Plant volatiles not only have multiple defense functions against herbivores, fungi, and bacteria, but also have been implicated in signaling within the plant and toward other organisms. Elucidating the function of individual plant volatiles will require more knowledge of their biosynthesis and regulation in response to external stimuli. By exploiting the variation of herbivore-induced volatiles among 26 maize ( Zea mays ) inbred lines, we conducted a nested association mapping and genome-wide association study (GWAS ) to identify a set of quantitative trait loci (QTLs) for investigating the pathways of volatile terpene production. The most significant identified QTL affects the emission of ( E )-nerolidol, linalool, and the two homoterpenes ( E )-3, 8-dimethyl-1, 4, 7-nonatriene (DMNT ) and ( E, E )-4, 8, 12-trimethyltrideca-1, 3, 7, 11-tetraene (TMTT ). GWAS associated a single nucleotide polymorphism in the promoter of the gene encoding the terpene synthase TPS2 with this QTL . Biochemical characterization of TPS2 verified that this plastid-localized enzyme forms linalool, ( E )-nerolidol, and ( E, E )-geranyllinalool. The subsequent conversion of ( E )-nerolidol into DMNT maps to a P450 monooxygenase, CYP92C5, which is capable of converting nerolidol into DMNT by oxidative degradation. A QTL influencing TMTT accumulation corresponds to a similar monooxygenase, CYP92C6, which is specific for the conversion of ( E, E )-geranyllinalool to TMTT . The DMNT biosynthetic pathway and both monooxygenases are distinct from those previously characterized for DMNT and TMTT synthesis in Arabidopsis thaliana, suggesting independent evolution of these enzymatic activities. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 10(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 10(2016)
- Issue Display:
- Volume 28, Issue 10 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 10
- Issue Sort Value:
- 2016-0028-0010-0000
- Page Start:
- 2651
- Page End:
- 2665
- Publication Date:
- 2016-09-23
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00919 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16318.xml