Remobilization of Phytol from Chlorophyll Degradation Is Essential for Tocopherol Synthesis and Growth of Arabidopsis. Issue 10 (9th October 2015)
- Record Type:
- Journal Article
- Title:
- Remobilization of Phytol from Chlorophyll Degradation Is Essential for Tocopherol Synthesis and Growth of Arabidopsis. Issue 10 (9th October 2015)
- Main Title:
- Remobilization of Phytol from Chlorophyll Degradation Is Essential for Tocopherol Synthesis and Growth of Arabidopsis
- Authors:
- vom Dorp, Katharina
Hölzl, Georg
Plohmann, Christian
Eisenhut, Marion
Abraham, Marion
Weber, Andreas P.M.
Hanson, Andrew D.
Dörmann, Peter - Abstract:
- Abstract : Tocopherol synthesis and growth of Arabidopsis require the activity of the phytyl-phosphate kinase VTE6 in the phosphorylation cascade of the phytol salvage pathway. Abstract: Phytol from chlorophyll degradation can be phosphorylated to phytyl-phosphate and phytyl-diphosphate, the substrate for tocopherol (vitamin E) synthesis. A candidate for the phytyl-phosphate kinase from Arabidopsis thaliana (At1g78620) was identified via a phylogeny-based approach. This gene was designated VITAMIN E DEFICIENT6 ( VTE6 ) because the leaves of the Arabidopsis vte6 mutants are tocopherol deficient. The vte6 mutant plants are incapable of photoautotrophic growth. Phytol and phytyl-phosphate accumulate, and the phytyl-diphosphate content is strongly decreased in vte6 leaves. Phytol feeding and enzyme assays with Arabidopsis and recombinant Escherichia coli cells demonstrated that VTE6 has phytyl-P kinase activity. Overexpression of VTE6 resulted in increased phytyl-diphosphate and tocopherol contents in seeds, indicating that VTE6 encodes phytyl-phosphate kinase. The severe growth retardation of vte6 mutants was partially rescued by introducing the phytol kinase mutation vte5 . Double mutant plants ( vte5 vte6 ) are tocopherol deficient and contain more chlorophyll, but reduced amounts of phytol and phytyl-phosphate compared with vte6 mutants, suggesting that phytol or phytyl-phosphate are detrimental to plant growth. Therefore, VTE6 represents the missing phytyl-phosphate kinase,Abstract : Tocopherol synthesis and growth of Arabidopsis require the activity of the phytyl-phosphate kinase VTE6 in the phosphorylation cascade of the phytol salvage pathway. Abstract: Phytol from chlorophyll degradation can be phosphorylated to phytyl-phosphate and phytyl-diphosphate, the substrate for tocopherol (vitamin E) synthesis. A candidate for the phytyl-phosphate kinase from Arabidopsis thaliana (At1g78620) was identified via a phylogeny-based approach. This gene was designated VITAMIN E DEFICIENT6 ( VTE6 ) because the leaves of the Arabidopsis vte6 mutants are tocopherol deficient. The vte6 mutant plants are incapable of photoautotrophic growth. Phytol and phytyl-phosphate accumulate, and the phytyl-diphosphate content is strongly decreased in vte6 leaves. Phytol feeding and enzyme assays with Arabidopsis and recombinant Escherichia coli cells demonstrated that VTE6 has phytyl-P kinase activity. Overexpression of VTE6 resulted in increased phytyl-diphosphate and tocopherol contents in seeds, indicating that VTE6 encodes phytyl-phosphate kinase. The severe growth retardation of vte6 mutants was partially rescued by introducing the phytol kinase mutation vte5 . Double mutant plants ( vte5 vte6 ) are tocopherol deficient and contain more chlorophyll, but reduced amounts of phytol and phytyl-phosphate compared with vte6 mutants, suggesting that phytol or phytyl-phosphate are detrimental to plant growth. Therefore, VTE6 represents the missing phytyl-phosphate kinase, linking phytol release from chlorophyll with tocopherol synthesis. Moreover, tocopherol synthesis in leaves depends on phytol derived from chlorophyll, not on de novo synthesis of phytyl-diphosphate from geranylgeranyl-diphosphate. … (more)
- Is Part Of:
- The Plant Cell. Volume 27:Issue 10(2015)
- Journal:
- The Plant Cell
- Issue:
- Volume 27:Issue 10(2015)
- Issue Display:
- Volume 27, Issue 10 (2015)
- Year:
- 2015
- Volume:
- 27
- Issue:
- 10
- Issue Sort Value:
- 2015-0027-0010-0000
- Page Start:
- 2846
- Page End:
- 2859
- Publication Date:
- 2015-10-09
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00395 ↗
- 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