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Structural cell-wall proteins in protoxylem development: evidence for a repair process mediated by a glycine-rich protein.
Structural cell-wall proteins in protoxylem development: evidence for a repair process mediated by a glycine-rich protein.
- Source :
-
The Plant journal : for cell and molecular biology [Plant J] 1997 Jul; Vol. 12 (1), pp. 97-111. - Publication Year :
- 1997
-
Abstract
- Polyclonal antibodies were used to localize structural cell-wall proteins in differentiating protoxylem elements in etiolated bean and soybean hypocotyls at the light- and electron-microscopic level. A proline-rich protein was localized in the lignified secondary walls, but not in the primary walls of protoxylem elements, which remain unlignified, as shown with lignin-specific antibodies. Secretion of the proline-rich protein was observed during lignification in different cell types. A glycine-rich protein (GRP1.8) was specifically localized in the modified primary walls of mature protoxylem elements and in cell corners between xylem elements and xylem parenchyma cells. The protein was secreted by Golgi bodies both in protoxylem cells after the lignification of their secondary walls and in the surrounding xylem parenchyma cells. The modified primary walls of protoxylem elements were visualized under the light microscope as filaments or sheets staining distinctly with the protein stain Coomassie blue. Electron micrographs of these walls show that they are composed of an amorphous material of moderate electron-density and of polysaccharide microfibrils. These materials form a three-dimensional network, interconnecting the ring- or spiral-shaped secondary wall thickenings of protoxylem elements and xylem parenchyma cells. The results demonstrate that the modified primary walls of protoxylem cells are not simply breakdown products due to partial hydrolysis and passive elongation, as believed until now. Extensive repair processes produces cell walls with unique staining properties. It is concluded that these walls are unusually rich in protein and therefore have special chemical and physical properties.
- Subjects :
- Antibodies
Cell Wall physiology
Fabaceae cytology
Fabaceae physiology
Glycine
Golgi Apparatus ultrastructure
Membrane Proteins physiology
Microscopy, Electron
Microscopy, Immunoelectron
Plant Proteins physiology
Polysaccharides analysis
Recombinant Fusion Proteins analysis
Glycine max cytology
Glycine max physiology
Glycine max ultrastructure
Cell Wall ultrastructure
Fabaceae ultrastructure
Membrane Proteins analysis
Plant Proteins analysis
Plants, Medicinal
Subjects
Details
- Language :
- English
- ISSN :
- 0960-7412
- Volume :
- 12
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- The Plant journal : for cell and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 9263454
- Full Text :
- https://doi.org/10.1046/j.1365-313x.1997.12010097.x