Reduced Biosynthesis of Digalactosyldiacylglycerol, a Major Chloroplast Membrane Lipid, Leads to Oxylipin Overproduction and Phloem Cap Lignification in Arabidopsis. Issue 1 (31st December 2015)
- Record Type:
- Journal Article
- Title:
- Reduced Biosynthesis of Digalactosyldiacylglycerol, a Major Chloroplast Membrane Lipid, Leads to Oxylipin Overproduction and Phloem Cap Lignification in Arabidopsis. Issue 1 (31st December 2015)
- Main Title:
- Reduced Biosynthesis of Digalactosyldiacylglycerol, a Major Chloroplast Membrane Lipid, Leads to Oxylipin Overproduction and Phloem Cap Lignification in Arabidopsis
- Authors:
- Lin, Yang-Tsung
Chen, Lih-Jen
Herrfurth, Cornelia
Feussner, Ivo
Li, Hsou-min - Abstract:
- Abstract : The short inflorescence stem phenotype of a chloroplast lipid mutant is caused by jasmonic acid overproduction, demonstrating a direct link between the biosynthesis of this lipid and jasmonic acid. Abstract: DIGALACTOSYLDIACYLGLYCEROL SYNTHASE1 (DGD1) is a chloroplast outer membrane protein responsible for the biosynthesis of the lipid digalactosyldiacylglycerol (DGDG ) from monogalactosyldiacylglycerol (MGDG ). The Arabidopsis thaliana dgd1 mutants have a greater than 90% reduction in DGDG content, reduced photosynthesis, and altered chloroplast morphology. However, the most pronounced visible phenotype is the extremely short inflorescence stem, but how deficient DGDG biosynthesis causes this phenotype is unclear. We found that, in dgd1 mutants, phloem cap cells were lignified and jasmonic acid (JA )-responsive genes were highly upregulated under normal growth conditions. The coronative insensitive1 dgd1 and allene oxide synthase dgd1 double mutants no longer exhibited the short inflorescence stem and lignification phenotypes but still had the same lipid profile and reduced photosynthesis as dgd1 single mutants. Hormone and lipidomics analyses showed higher levels of JA, JA -isoleucine, 12-oxo-phytodienoic acid, and arabidopsides in dgd1 mutants. Transcript and protein level analyses further suggest that JA biosynthesis in dgd1 is initially activated through the increased expression of genes encoding 13-lipoxygenases (LOXs) and phospholipase A-Iγ3Abstract : The short inflorescence stem phenotype of a chloroplast lipid mutant is caused by jasmonic acid overproduction, demonstrating a direct link between the biosynthesis of this lipid and jasmonic acid. Abstract: DIGALACTOSYLDIACYLGLYCEROL SYNTHASE1 (DGD1) is a chloroplast outer membrane protein responsible for the biosynthesis of the lipid digalactosyldiacylglycerol (DGDG ) from monogalactosyldiacylglycerol (MGDG ). The Arabidopsis thaliana dgd1 mutants have a greater than 90% reduction in DGDG content, reduced photosynthesis, and altered chloroplast morphology. However, the most pronounced visible phenotype is the extremely short inflorescence stem, but how deficient DGDG biosynthesis causes this phenotype is unclear. We found that, in dgd1 mutants, phloem cap cells were lignified and jasmonic acid (JA )-responsive genes were highly upregulated under normal growth conditions. The coronative insensitive1 dgd1 and allene oxide synthase dgd1 double mutants no longer exhibited the short inflorescence stem and lignification phenotypes but still had the same lipid profile and reduced photosynthesis as dgd1 single mutants. Hormone and lipidomics analyses showed higher levels of JA, JA -isoleucine, 12-oxo-phytodienoic acid, and arabidopsides in dgd1 mutants. Transcript and protein level analyses further suggest that JA biosynthesis in dgd1 is initially activated through the increased expression of genes encoding 13-lipoxygenases (LOXs) and phospholipase A-Iγ3 (At1g51440), a plastid lipase with a high substrate preference for MGDG, and is sustained by further increases in LOX and allene oxide cyclase mRNA and protein levels. Our results demonstrate a link between the biosynthesis of DGDG and JA . … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 1(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 1(2016)
- Issue Display:
- Volume 28, Issue 1 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 1
- Issue Sort Value:
- 2016-0028-0001-0000
- Page Start:
- 219
- Page End:
- 232
- Publication Date:
- 2015-12-31
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.01002 ↗
- 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:
- 16319.xml