A novel extracellular matrix protein from tomato associated with lignified secondary cell walls.

Domingo, Concha; Gómez, María Dolores; Cañas, Luis A.; Hernández-Yago, José; Conejero, Vicente; Vera, Pablo

doi:10.1105/tpc.6.8.1035

Cited by 39 publications

(37 citation statements)

References 39 publications

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“…The GST/PTGRP junction was sequenced to ensure that this fragment was in the correct reading frame. The pGEX-PTGRP plasmid was used to produce the GST/PTGRP fusion protein according to the method of Domingo et al (1994). Escherichia coli strain DH5 (BRL, Gaithersburg, MD) were transformed with pGEX/PTGRP and grown at 37°C until the A 600 reached 0.7.…”

Section: Fusion Protein Construct Expression and Purificationmentioning

confidence: 99%

A Proline-, Threonine-, and Glycine-Rich Protein Down-Regulated by Drought Is Localized in the Cell Wall of Xylem Elements

Harrak

Chamberland²,

Plante³

et al. 1999

Plant Physiology

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A cDNA clone encoding a proline-, threonine-, and glycine-rich protein (PTGRP) was isolated from a wild tomato species (Lycopersicon chilense) (L.X. Yu, H. Chamberland, J.G. Lafontain, Z. Tabaeizadeh [1996] Genome 39: 1185-1193). Northern-blot analysis and in situ hybridization studies revealed that PTGRP is downregulated by drought stress. The level of the mRNA in leaves and stems of 8-d drought-stressed plants decreased 5-to 10-fold compared with that in regularly watered plants. The mRNA reaccumulated when drought-stressed plants were rewatered. Antibodies raised against a glutathione S-transferase/PTGRP fusion protein were used to elucidate the subcellular localization of the protein by immunogold labeling. In regularly watered L. chilense plants, PTGRP protein was found to be localized in xylem pit membranes and disintegrated primary walls. Examination of sections from drought-stressed plants revealed a significant decrease in the levels of labeling. In these samples, only a few scattered gold particles were detected in the same areas. In the leaf tissues of plants that had been rewatered for 3 d following an 8-d drought stress, the labeling pattern was similar to that of the regularly watered plants. To our knowledge, PTGRP is the first droughtregulated protein that has been precisely localized in the cell wall.

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Section: Fusion Protein Construct Expression and Purificationmentioning

confidence: 99%

A Proline-, Threonine-, and Glycine-Rich Protein Down-Regulated by Drought Is Localized in the Cell Wall of Xylem Elements

Harrak

Chamberland²,

Plante³

et al. 1999

Plant Physiology

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“…However, no protein targets responsible for the observed binding were characterized biochemically (Sherrier and VandenBosch, 1994). Thus, to our knowledge the only known examples of biochemical and structural localization of proteins in secondary cell walls are Hyp-rich, extensin-like protein from loblolly pine (Pinus taeda L.) (Bao et al, 1992) and Tyr-and Lys-rich protein from tomato (Lycopersicon esculentum L.) (Domingo et al, 1994).…”

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confidence: 99%

Secondary Cell-Wall-Specific Glycoprotein(s) from French Bean Hypocotyls

Wojtaszek

Bolwell

1995

Plant Physiol.

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Specific labeling of secondary cell walls of tracheary elements and of xylary and phloem fibers has been observed when wheat germ agglutinin (WCA) and anti-WCA antibodies were used during ultrastructural studies of French bean (Phaseolus vulgaris L.) hypocotyls. In this report we demonstrate that at least part of this labeling is due to the presence of secondary cell-wall-specific glycoproteins. Three major nove1 glycoproteins with relative molecular weights of 55,000, 86,000, and 90,000, purified by means of WCA-Sepharose affinity chromatography, have been characterized. Their amino acid composition indicates that they are not the members of known classes of structural cell-wall proteins, since they contain no hydroxyproline, a lower level of glycine than seen in glycine-rich proteins, and very little proline. N-terminal sequences of all three proteins show no significant homology with other proteins. Antibodies were raised against electrophoretically pure 90-kD glycoprotein. These were used to localize this protein in secondary cell walls of xylem tracheary elements and in xylary and phloem fibers, i.e. in the same compartments where labeling with WCA has been observed. To our knowledge this is one of the first biochemical and ultrastructural demonstrations of secondary cellwall-specific gl ycoproteins.

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“…From the fifth internode downwards in the stem of a grown tomato plant is the region where secondary growth seems to be taking place and where increased diameter and thickening of the stem is observed. In these older internodes phloroglucinol staining of lignin is apparent (not shown) and coincides with the internodes where a lignin peroxidase gene becomes transcriptionally active (Domingo et al, 1994).…”

Section: Expression Of Vahox1 and Dna-related Sequencesmentioning

confidence: 99%

“…A tomato genomic DNA library constructed in X-EMBL3 (Clontech) was screened with a radiolabeled p45 cDNA probe, and the positive clones were isolated and purified following standard techniques (Maniatis et aL, 1982). DNA sequencing and computer-assisted comparison of DNA sequences were as described before (Domingo et al, 1994;Tornero et al, 1994).…”

Section: Dna and Rna Isolation And Gel-blot Analysismentioning

confidence: 99%

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Phloem‐specific expression of a plant homeobox gene during secondary phases of vascular development

Tornero

Conejero

Vera³

1996

The Plant Journal

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SummaryThis paper reports the isolation and characterization of a homeobox gene (VAHOXI) from Lycopersicon esculentum encoding a homeodomain protein that contains a leucine zipper motif. The bipartite homeodomain-leucine zipper (HD-Zip) motif has only been found in homeobox genes from dicotyledonous plants, indicating that this type of transcription factor regulates particular developmental processes in these plant species. Here, the genomic organization, sequence comparison and expression analysis of VAHOX1 are described. Transcriptional fusion of the 5' promoter region of VAHOX1 with the reporter GUS gene (VAHOX1-GUS) and expression analysis of this construct in transgenic plants indicates that VAHOX1 is specifically expressed in the phloem during phases of secondary growth. Unlike other plant homeobox genes, VAHOX1 does not appear to be expressed in meristems, and the function of VAHOX1 is considered a likely candidate molecule that may participate in the regulation of the identity and/or activity of phloem tissues during secondary phases of vascular development.

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A novel extracellular matrix protein from tomato associated with lignified secondary cell walls.

Cited by 39 publications

References 39 publications

A Proline-, Threonine-, and Glycine-Rich Protein Down-Regulated by Drought Is Localized in the Cell Wall of Xylem Elements

A Proline-, Threonine-, and Glycine-Rich Protein Down-Regulated by Drought Is Localized in the Cell Wall of Xylem Elements

Secondary Cell-Wall-Specific Glycoprotein(s) from French Bean Hypocotyls

Phloem‐specific expression of a plant homeobox gene during secondary phases of vascular development

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