UUAT1 Is a Golgi-Localized UDP-Uronic Acid Transporter That Modulates the Polysaccharide Composition of Arabidopsis Seed Mucilage. Issue 1 (6th January 2017)
- Record Type:
- Journal Article
- Title:
- UUAT1 Is a Golgi-Localized UDP-Uronic Acid Transporter That Modulates the Polysaccharide Composition of Arabidopsis Seed Mucilage. Issue 1 (6th January 2017)
- Main Title:
- UUAT1 Is a Golgi-Localized UDP-Uronic Acid Transporter That Modulates the Polysaccharide Composition of Arabidopsis Seed Mucilage
- Authors:
- Saez-Aguayo, Susana
Rautengarten, Carsten
Temple, Henry
Sanhueza, Dayan
Ejsmentewicz, Troy
Sandoval-Ibañez, Omar
Doñas, Daniela
Parra-Rojas, Juan Pablo
Ebert, Berit
Lehner, Arnaud
Mollet, Jean-Claude
Dupree, Paul
Scheller, Henrik V.
Heazlewood, Joshua L.
Reyes, Francisca C.
Orellana, Ariel - Abstract:
- Abstract : Screening of Arabidopsis mutants with altered seed mucilage allowed identification of UUAT1, a Golgi-localized protein that transports UDP-glucuronic acid and plays a role in the biosynthesis of pectin. Abstract: UDP-glucuronic acid (UDP-GlcA ) is the precursor of many plant cell wall polysaccharides and is required for production of seed mucilage. Following synthesis in the cytosol, it is transported into the lumen of the Golgi apparatus, where it is converted to UDP-galacturonic acid (UDP-GalA), UDP-arabinose, and UDP-xylose. To identify the Golgi-localized UDP-GlcA transporter, we screened Arabidopsis thaliana mutants in genes coding for putative nucleotide sugar transporters for altered seed mucilage, a structure rich in the GalA-containing polysaccharide rhamnogalacturonan I. As a result, we identified UUAT1, which encodes a Golgi-localized protein that transports UDP-GlcA and UDP-GalA in vitro. The seed coat of uuat1 mutants had less GalA, rhamnose, and xylose in the soluble mucilage, and the distal cell walls had decreased arabinan content. Cell walls of other organs and cells had lower arabinose levels in roots and pollen tubes, but no differences were observed in GalA or xylose contents. Furthermore, the GlcA content of glucuronoxylan in the stem was not affected in the mutant. Interestingly, the degree of homogalacturonan methylation increased in uuat1 . These results suggest that this UDP-GlcA transporter plays a key role defining the seed mucilageAbstract : Screening of Arabidopsis mutants with altered seed mucilage allowed identification of UUAT1, a Golgi-localized protein that transports UDP-glucuronic acid and plays a role in the biosynthesis of pectin. Abstract: UDP-glucuronic acid (UDP-GlcA ) is the precursor of many plant cell wall polysaccharides and is required for production of seed mucilage. Following synthesis in the cytosol, it is transported into the lumen of the Golgi apparatus, where it is converted to UDP-galacturonic acid (UDP-GalA), UDP-arabinose, and UDP-xylose. To identify the Golgi-localized UDP-GlcA transporter, we screened Arabidopsis thaliana mutants in genes coding for putative nucleotide sugar transporters for altered seed mucilage, a structure rich in the GalA-containing polysaccharide rhamnogalacturonan I. As a result, we identified UUAT1, which encodes a Golgi-localized protein that transports UDP-GlcA and UDP-GalA in vitro. The seed coat of uuat1 mutants had less GalA, rhamnose, and xylose in the soluble mucilage, and the distal cell walls had decreased arabinan content. Cell walls of other organs and cells had lower arabinose levels in roots and pollen tubes, but no differences were observed in GalA or xylose contents. Furthermore, the GlcA content of glucuronoxylan in the stem was not affected in the mutant. Interestingly, the degree of homogalacturonan methylation increased in uuat1 . These results suggest that this UDP-GlcA transporter plays a key role defining the seed mucilage sugar composition and that its absence produces pleiotropic effects in this component of the plant extracellular matrix. … (more)
- Is Part Of:
- The Plant Cell. Volume 29:Issue 1(2017)
- Journal:
- The Plant Cell
- Issue:
- Volume 29:Issue 1(2017)
- Issue Display:
- Volume 29, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 29
- Issue:
- 1
- Issue Sort Value:
- 2017-0029-0001-0000
- Page Start:
- 129
- Page End:
- 143
- Publication Date:
- 2017-01-06
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.16.00465 ↗
- 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:
- 16314.xml