title: Structural cell-wall proteins in protoxylem development: evidence for a repair process mediated by a glycine-rich protein.
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.
authors.affiliation: Institute of Plant Biology, University of Freiburg, Switzerland. ulrich.ryser@unifr.ch
authors.forename: U
authors.initials: U
authors.lastname: Ryser
authors.forename: M
authors.initials: M
authors.lastname: Schorderet
authors.forename: G F
authors.initials: GF
authors.lastname: Zhao
authors.forename: D
authors.initials: D
authors.lastname: Studer
authors.forename: K
authors.initials: K
authors.lastname: Ruel
authors.forename: G
authors.initials: G
authors.lastname: Hauf
authors.forename: B
authors.initials: B
authors.lastname: Keller
mesh_terms: D000906:Antibodies; D002473:Cell Wall / Q000502:physiology / Q000648:ultrastructure*; D007887:Fabaceae / Q000166:cytology / Q000502:physiology / Q000648:ultrastructure*; D005998:Glycine; D006056:Golgi Apparatus / Q000648:ultrastructure; D008565:Membrane Proteins / Q000032:analysis* / Q000502:physiology; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D010940:Plant Proteins / Q000032:analysis* / Q000502:physiology; D010946:Plants, Medicinal; D011134:Polysaccharides / Q000032:analysis; D011993:Recombinant Fusion Proteins / Q000032:analysis; D013025:Glycine max / Q000166:cytology / Q000502:physiology / Q000648:ultrastructure
chemical_list: D000906:Antibodies; D008565:Membrane Proteins; D010940:Plant Proteins; D011134:Polysaccharides; D011993:Recombinant Fusion Proteins; D005998:Glycine