arabinogalactan/nicotiana

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Tomato LeAGP-1 is a plasma membrane-bound, glycosylphosphatidylinositol-anchored arabinogalactan-protein.

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Arabinogalactan-proteins (AGPs) are a class of highly glycosylated, hydroxyproline-rich glycoproteins that function in plant growth and development. Tomato LeAGP-1 represents a major AGP expressed in cultured cells and plants. Based on cDNA and amino acid sequence analyses along with carbohydrate

Glycosylation motifs that direct arabinogalactan addition to arabinogalactan-proteins.

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Hydroxyproline (Hyp)-rich glycoproteins (HRGPs) participate in all aspects of plant growth and development. HRGPs are generally highly O-glycosylated through the Hyp residues, which means carbohydrates help define the interactive molecular surface and, hence, HRGP function. The Hyp contiguity

A style-specific hydroxyproline-rich glycoprotein with properties of both extensins and arabinogalactan proteins.

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A basic, hydroxyproline-rich glycoprotein (molecular mass 120 kDa) has been purified from the styles of Nicotiana alata. An antibody, specific for the protein backbone (molecular mass 78 kDa) of the glycoprotein, was used to demonstrate that the glycoprotein is a soluble, style-specific component

Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies.

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We investigated the subcellular distribution of antigenic sites immunoreactive to the monoclonal antibody 16.4B4 (PM Norman, VPM Wingate, MS Fitter, CJ Lamb [1986] Planta 167: 452-459) in tobacco (Nicotiana tabacum) leaf cells. This antibody is directed against a glycan epitope in a family of plasma

Identification and characterization of in vitro galactosyltransferase activities involved in arabinogalactan-protein glycosylation in tobacco and Arabidopsis.

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Arabinogalactan-proteins (AGPs) are highly glycosylated hydroxyproline (Hyp)-rich glycoproteins that are frequently characterized by the presence of [Alanine-Hyp] ([AO]) repetitive units. AGP galactosyltransferase (GalT) activities in tobacco (Nicotiana tabacum) and Arabidopsis (Arabidopsis

Arabinogalactan biosynthesis: Implication of AtGALT29A enzyme activity regulated by phosphorylation and co-localized enzymes for nucleotide sugar metabolism in the compartments outside of the Golgi apparatus.

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Arabinogalactan proteins are abundant cell surface proteoglycans in plants and are implicated to act as developmental markers during plant growth. We previously reported that AtGALT31A, AtGALT29A, and AtGLCAT14A-C, which are involved in the biosynthesis of arabinogalactan proteins, localize not only

Pollen proteins bind to the C-terminal domain of Nicotiana alata pistil arabinogalactan proteins.

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Pollen tube growth is influenced by interaction between pollen proteins and the pistil extracellular matrix. The transmitting tract-specific glycoprotein (NaTTS) and 120-kDa glycoprotein (120K) are two pistil arabinogalactan proteins (AGPs) that share a conserved C-terminal domain (CTD) and directly

Tomato LeAGP-1 arabinogalactan-protein purified from transgenic tobacco corroborates the Hyp contiguity hypothesis.

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Functional analysis of the hyperglycosylated arabinogalactan-proteins (AGPs) attempts to relate biological roles to the molecular properties that result largely from O-Hyp glycosylation putatively coded by the primary sequence. The Hyp contiguity hypothesis predicts contiguous Hyp residues as

Characterization of PhPRP1, a histidine domain arabinogalactan protein from Petunia hybrida pistils.

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An arabinogalactan protein, PhPRP1, was purified from Petunia hybrida pistils and shown to be orthologous to TTS-1 and TTS-2 from Nicotiana tabacum and NaTTS from Nicotiana alata. Sequence comparisons among these proteins, and CaPRP1 from Capsicum annuum, reveal a conserved histidine-rich domain and

A chimeric arabinogalactan protein promotes somatic embryogenesis in cotton cell culture.

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Arabinogalactan proteins (AGPs) are a family of extracellular plant proteoglycans implicated in many aspects of plant growth and development, including in vitro somatic embryogenesis (SE). We found that specific AGPs were produced by cotton (Gossypium hirsutum) calli undergoing SE and that when

[The localization of arabinogalactan-proteins in stigma and style of Nicotiana tabacum L].

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The distribution patterns of arabinogalactan-proteins (AGPs) in stigma and style of Nicotiana tabacum L. were studied with western blotting, immunohistochemistry and ultracytochemistry techniques. The results showed abundant AGPs accumulated in the stigmas and styles (Fig.1, Plate I). AGPs were

Periodic deposition of arabinogalactan epitopes in the cell wall of pollen tubes of Nicotiana tabacum L.

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The monoclonal antibodies MAC 207 and JIM 8, recognizing arabinogalactan epitopes, were used to localize the corresponding antigenic sites in pollen tubes of Nicotiana tabacum L. grown in vitro or semi in vivo. The analysis of the immunofluorescence labelling was performed by means of confocal laser

Structure of the glycosylphosphatidylinositol anchor of an arabinogalactan protein from Pyrus communis suspension-cultured cells.

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Arabinogalactan proteins (AGPs) are proteoglycans of higher plants, which are implicated in growth and development. We recently have shown that two AGPs, NaAGP1 (from Nicotiana alata styles) and PcAGP1 (from Pyrus communis cell suspension culture), are modified by the addition of a

Molecular cloning of cDNAs encoding the protein backbones of arabinogalactan-proteins from the filtrate of suspension-cultured cells of Pyrus communis and Nicotiana alata.

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This paper reports the isolation of cDNAs encoding the protein backbone of two arabinogalactan-proteins (AGPs), one from pear cell suspension cultures (AGPPc2) and the other from suspension cultures of Nicotiana alata (AGPNa2). The proteins encoded by these cDNAs are quite different from the

Molecular characterization of a stigma-specific gene encoding an arabinogalactan-protein (AGP) from Nicotiana alata.

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Arabinogalactan-proteins (AGPs) were isolated from the pistils of Nicotiana alata, deglycosylated, and the protein backbones fractionated by reversed-phase HPLC as previously reported. A major fraction, RT35 was isolated and peptide sequences were obtained after protease digestion. A gene-specific

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