Glycome and Proteome Components of Golgi Membranes Are Common between Two Angiosperms with Distinct Cell-Wall Structures. Issue 5 (26th March 2019)
- Record Type:
- Journal Article
- Title:
- Glycome and Proteome Components of Golgi Membranes Are Common between Two Angiosperms with Distinct Cell-Wall Structures. Issue 5 (26th March 2019)
- Main Title:
- Glycome and Proteome Components of Golgi Membranes Are Common between Two Angiosperms with Distinct Cell-Wall Structures
- Authors:
- Okekeogbu, Ikenna O.
Pattathil, Sivakumar
González Fernández-Niño, Susana M.
Aryal, Uma K.
Penning, Bryan W.
Lao, Jeemeng
Heazlewood, Joshua L.
Hahn, Michael G.
McCann, Maureen C.
Carpita, Nicholas C. - Abstract:
- Abstract : Despite the large differences in the polysaccharide constituents of the cell walls of eudicots and grasses, the glycome profiles are common to Golgi membranes from both Arabidopsis and maize. Abstract: The plant endoplasmic reticulum-Golgi apparatus is the site of synthesis, assembly, and trafficking of all noncellulosic polysaccharides, proteoglycans, and proteins destined for the cell wall. As grass species make cell walls distinct from those of dicots and noncommelinid monocots, it has been assumed that the differences in cell-wall composition stem from differences in biosynthetic capacities of their respective Golgi. However, immunosorbence-based screens and carbohydrate linkage analysis of polysaccharides in Golgi membranes, enriched by flotation centrifugation from etiolated coleoptiles of maize ( Zea mays ) and leaves of Arabidopsis ( Arabidopsis thaliana ), showed that arabinogalactan-proteins and arabinans represent substantial portions of the Golgi-resident polysaccharides not typically found in high abundance in cell walls of either species. Further, hemicelluloses accumulated in Golgi at levels that contrasted with those found in their respective cell walls, with xyloglucans enriched in maize Golgi, and xylans enriched in Arabidopsis. Consistent with this finding, maize Golgi membranes isolated by flotation centrifugation and enriched further by free-flow electrophoresis, yielded >200 proteins known to function in the biosynthesis and metabolism ofAbstract : Despite the large differences in the polysaccharide constituents of the cell walls of eudicots and grasses, the glycome profiles are common to Golgi membranes from both Arabidopsis and maize. Abstract: The plant endoplasmic reticulum-Golgi apparatus is the site of synthesis, assembly, and trafficking of all noncellulosic polysaccharides, proteoglycans, and proteins destined for the cell wall. As grass species make cell walls distinct from those of dicots and noncommelinid monocots, it has been assumed that the differences in cell-wall composition stem from differences in biosynthetic capacities of their respective Golgi. However, immunosorbence-based screens and carbohydrate linkage analysis of polysaccharides in Golgi membranes, enriched by flotation centrifugation from etiolated coleoptiles of maize ( Zea mays ) and leaves of Arabidopsis ( Arabidopsis thaliana ), showed that arabinogalactan-proteins and arabinans represent substantial portions of the Golgi-resident polysaccharides not typically found in high abundance in cell walls of either species. Further, hemicelluloses accumulated in Golgi at levels that contrasted with those found in their respective cell walls, with xyloglucans enriched in maize Golgi, and xylans enriched in Arabidopsis. Consistent with this finding, maize Golgi membranes isolated by flotation centrifugation and enriched further by free-flow electrophoresis, yielded >200 proteins known to function in the biosynthesis and metabolism of cell-wall polysaccharides common to all angiosperms, and not just those specific to cell-wall type. We propose that the distinctive compositions of grass primary cell walls compared with other angiosperms result from differential gating or metabolism of secreted polysaccharides post-Golgi by an as-yet unknown mechanism, and not necessarily by differential expression of genes encoding specific synthase complexes. … (more)
- Is Part Of:
- The Plant Cell. Volume 31:Issue 5(2019)
- Journal:
- The Plant Cell
- Issue:
- Volume 31:Issue 5(2019)
- Issue Display:
- Volume 31, Issue 5 (2019)
- Year:
- 2019
- Volume:
- 31
- Issue:
- 5
- Issue Sort Value:
- 2019-0031-0005-0000
- Page Start:
- 1094
- Page End:
- 1112
- Publication Date:
- 2019-03-26
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.18.00755 ↗
- 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:
- 19712.xml