RUBY, a Putative Galactose Oxidase, Influences Pectin Properties and Promotes Cell-To-Cell Adhesion in the Seed Coat Epidermis of Arabidopsis. Issue 4 (8th March 2019)
- Record Type:
- Journal Article
- Title:
- RUBY, a Putative Galactose Oxidase, Influences Pectin Properties and Promotes Cell-To-Cell Adhesion in the Seed Coat Epidermis of Arabidopsis. Issue 4 (8th March 2019)
- Main Title:
- RUBY, a Putative Galactose Oxidase, Influences Pectin Properties and Promotes Cell-To-Cell Adhesion in the Seed Coat Epidermis of Arabidopsis
- Authors:
- Šola, Krešimir
Gilchrist, Erin J.
Ropartz, David
Wang, Lisa
Feussner, Ivo
Mansfield, Shawn D.
Ralet, Marie-Christine
Haughn, George W. - Abstract:
- Abstract : A putative galactose oxidase, RUBY, promotes cell-to-cell adhesion between seed coat epidermal cells and modifies galactosylated RG-I pectin in the seed coat mucilage of Arabidopsis. Abstract: Cell-to-cell adhesion is essential for establishment of multicellularity. In plants, such adhesion is mediated through a middle lamella composed primarily of pectic polysaccharides. The molecular interactions that influence cell-to-cell adhesion are not fully understood. We have used Arabidopsis ( Arabidopsis thaliana ) seed coat mucilage as a model system to investigate interactions between cell wall carbohydrates. Using a forward-genetic approach, we have discovered a gene, RUBY PARTICLES IN MUCILAGE ( RUBY ), encoding a protein that is annotated as a member of the Auxiliary Activity 5 (AA5) family of Carbohydrate-Active Enzymes (Gal/glyoxal oxidases) and is secreted to the apoplast late in the differentiation of seed coat epidermal cells. We show that RUB Y is required for the Gal oxidase activity of intact seeds; the oxidation of Gal in side-chains of rhamnogalacturonan-I (RG-I) present in mucilage-modified2 ( mum2 ) mucilage, but not in wild-type mucilage; the retention of branched RG-I in the seed following extrusion; and the enhancement of cell-to-cell adhesion in the seed coat epidermis. These data support the hypothesis that RUBY is a Gal oxidase that strengthens pectin cohesion within the middle lamella, and possibly the mucilage of wild-type seed coat epidermalAbstract : A putative galactose oxidase, RUBY, promotes cell-to-cell adhesion between seed coat epidermal cells and modifies galactosylated RG-I pectin in the seed coat mucilage of Arabidopsis. Abstract: Cell-to-cell adhesion is essential for establishment of multicellularity. In plants, such adhesion is mediated through a middle lamella composed primarily of pectic polysaccharides. The molecular interactions that influence cell-to-cell adhesion are not fully understood. We have used Arabidopsis ( Arabidopsis thaliana ) seed coat mucilage as a model system to investigate interactions between cell wall carbohydrates. Using a forward-genetic approach, we have discovered a gene, RUBY PARTICLES IN MUCILAGE ( RUBY ), encoding a protein that is annotated as a member of the Auxiliary Activity 5 (AA5) family of Carbohydrate-Active Enzymes (Gal/glyoxal oxidases) and is secreted to the apoplast late in the differentiation of seed coat epidermal cells. We show that RUB Y is required for the Gal oxidase activity of intact seeds; the oxidation of Gal in side-chains of rhamnogalacturonan-I (RG-I) present in mucilage-modified2 ( mum2 ) mucilage, but not in wild-type mucilage; the retention of branched RG-I in the seed following extrusion; and the enhancement of cell-to-cell adhesion in the seed coat epidermis. These data support the hypothesis that RUBY is a Gal oxidase that strengthens pectin cohesion within the middle lamella, and possibly the mucilage of wild-type seed coat epidermal cells, through oxidation of RG-I Gal side-chains. … (more)
- Is Part Of:
- The Plant Cell. Volume 31:Issue 4(2019)
- Journal:
- The Plant Cell
- Issue:
- Volume 31:Issue 4(2019)
- Issue Display:
- Volume 31, Issue 4 (2019)
- Year:
- 2019
- Volume:
- 31
- Issue:
- 4
- Issue Sort Value:
- 2019-0031-0004-0000
- Page Start:
- 809
- Page End:
- 831
- Publication Date:
- 2019-03-08
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.18.00954 ↗
- 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:
- 19603.xml