Comparative localization of three classes of cell wall proteins

Ye, Zheng‐Hua; Song, Yanru; Marcus, Abraham; Varner, Joseph E.

doi:10.1046/j.1365-313x.1991.00175.x

Cited by 28 publications

(55 citation statements)

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“…In some instances, genes have been cloned whose open reading frames predict structural roles for their products once inserted in the cell wall (Condit and Meagher, 1986). Tissue printing has shown cell and tissue specific location of hydroxyproline-rich glycoproteins (HRGPs) (Cassab and Varner, 1987;Hood et a/., 1991;Keller eta/., 1989;Ye and Varner, 1991). Sequences have been deduced for several of these proteins, and their sites of glycosylation and other post-translational alterations are being studied to give clues to the three-dimensional conformation and chemistry of these glycoproteins.…”

Section: Advances In Probing Wall Structurementioning

confidence: 99%

“…The data on appearance of extensins and their relationship to growth do not support this view. Extensin precursors can be seen very early in cell wall formation, even in walls of cells near the meristem (Ye and Varner, 1991), but a large increase in amount of extensin in the cell wall is associated with cessation of growth (Sadava et al, 1973). In some cells, a strong correlation is found between final cell length and amount of Hyp in the cell walls (Iraki etal., 1989c), whereas the correlation is not as obvious in other systems (Ye and Vamer, 1991).…”

Section: Structural Proteins and The Fixation Of Shapementioning

confidence: 99%

“…Like extensin, the cell wall GRP is recalcitrant to extraction, but antibodies have been raised against artificial peptides corresponding to hydrophilic regions outside of the pleated sheet. These antibodies localize the GRP precursors to protoxylern elements and other cells that eventually become lignified (Condit eta/., 1990;Keller et a/., 1989;Ye and Varner, 1991;Ye eta/., 1991). The GRP is wound-inducible (Condit and Meagher, 1987), but this protein and others may function in wound-induced xylogenesis rather than as a response to pathogen invasion.…”

Section: Structural Proteins and The Fixation Of Shapementioning

confidence: 99%

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Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth

1993

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SummaryAdvances in determination of polymer structure and in preservation of structure for electron microscopy provide the best view to date of how polysaccharides and structural proteins are organized into plant cell walls. The walls that form and partition dividing cells are modified chemically and structurally from the walls expanding to provide a cell with its functional form. In grasses, the chemical structure of the wall differs from that of all other flowering plant species that have been examined. Nevertheless, both types of wall must conform to the same physical laws. Cell expansion occurs via strictly regulated reorientation of each of the wall's components that first permits the wall to stretch in specific directions and then lock into final shape. This review integrates information on the chemical structure of individual polymers with data obtained from new techniques used to probe the arrangement of the polymers within the walls of individual cells. We provide structural models of two distinct types of walls in flowering plants consistent with the physical properties of the wall and its components.

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Section: Advances In Probing Wall Structurementioning

confidence: 99%

Section: Structural Proteins and The Fixation Of Shapementioning

confidence: 99%

Section: Structural Proteins and The Fixation Of Shapementioning

confidence: 99%

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Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth

1993

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“…PRPs were first identified as proteins that accumulate in the cell wall in response to physical damage (Chen and Varner, 1985;Tierney et al, 1988) and have subsequently been shown to be temporally regulated during plant development. PRP gene expression is associated with early stages of legume root nodule formation (Franssen et al, 1987;van de Wiel et al, 1990;Wilson et al, 1994), soybean seedling, leaf, stem, and seed coat development (Hong et al, 1989;Kleis-San Francisco and Tierney, 1990;Lindstrom and Vodkin, 1991;Ye et al, 1991), bean seedling growth (Sheng et al, 1991), and with early stages of tomato fruit development (Santino et al, 1997). The spatial pattern of PRP expression is also tightly regulated, as shown by in situ hybridization and reporter gene expression analysis (Wyatt et al, 1992;Suzuki et al, 1993).…”

mentioning

confidence: 99%

“…Immunohistochemical analyses using antibodies raised against SbPRP2 localized PRP accumulation in soybean to protoxylem cells within the root and xylem and phloem fibers within the stem, indicating that these proteins are critical for maintaining structural integrity of mature tissues (Ye et al, 1991). PRPs may play a similar role during seed development, since seed coat integrity appears to be altered in soybean lines that fail to accumulated these proteins within their cell walls (Nicholas et al, 1993).…”

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confidence: 99%

Characterization and Expression of Four Proline-Rich Cell Wall Protein Genes in Arabidopsis Encoding Two Distinct Subsets of Multiple Domain Proteins

1999

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We have characterized the molecular organization and expression of four proline-rich protein genes from Arabidopsis (AtPRPs). These genes predict two classes of cell wall proteins based on DNA sequence identity, repetitive motifs, and domain organization. AtPRP1 and AtPRP3 encode proteins containing an N-terminal PRPlike domain followed by a C-terminal domain that is biased toward P, T, Y, and K. AtPRP2 and AtPRP4 represent a second, novel group of PRP genes that encode two-domain proteins containing a nonrepetitive N-terminal domain followed by a PRP-like region rich in P, V, K, and C. Northern hybridization analysis indicated that AtPRP1 and AtPRP3 are exclusively expressed in roots, while transcripts encoding AtPRP2 and AtPRP4 were most abundant in aerial organs of the plant. Histochemical analyses of promoter/␤-glucuronidase fusions localized AtPRP3 expression to regions of the root containing root hairs. AtPRP2 and AtPRP4 expression was detected in expanding leaves, stems, flowers, and siliques. In addition, AtPRP4 expression was detected in stipules and during the early stages of lateral root formation. These studies support a model for involvement of PRPs in specifying cell-type-specific wall structures, and provide the basis for a genetic approach to dissect the function of PRPs during growth and development.

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Vascular expression of the grp1.8 promoter is controlled by three specific regulatory elements and one unspecific activating sequence

Keller

Heierli

1994

Plant Mol Biol

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The bean grp1.8 full-length promoter is specifically active in vascular tissue during normal development of tobacco. Deletion of a negative regulatory element resulted in ectopic activity of the promoter in cortical cells of hypocotyls, roots and stems. A 169 bp fragment (-205 to -36) of the grp1.8 promoter conferred vascular-specific expression to CaMV 35S minimal promoters whereas a 141 bp fragment (-205 to -64) strongly activated these minimal promoters both in vascular and cortical cells. These experiments defined a new regulatory element (VSE) that is essential for vascular-specific expression and is located between -64 and -36. The 141 bp grp1.8 promoter sequence had enhancer-like properties as it was active in both orientations. A 24 bp sequence (bp -119 to -96, corresponding to the SE1 regulatory element) enhanced expression from several minimal promoters strongly but unspecifically, whereas a 26 bp sequence (-98 to -73, corresponding to the RSE regulatory element) induced vascular-specific expression. Thus, the grp1.8 promoter is regulated by a combinatorial mechanism that can integrate the action of different, non-additively acting regulatory elements into vascular-specific expression.

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Comparative localization of three classes of cell wall proteins

Cited by 28 publications

References 0 publications

Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth

Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth

Characterization and Expression of Four Proline-Rich Cell Wall Protein Genes in Arabidopsis Encoding Two Distinct Subsets of Multiple Domain Proteins

Vascular expression of the grp1.8 promoter is controlled by three specific regulatory elements and one unspecific activating sequence

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