Characterization of oleosins in the pollen coat of Brassica oleracea.

Ruiter, R.K.; Eldik, G.J. van; Herpen, R.M.A. van; Schrauwen, J. A. M.; Wullems, G. J.

doi:10.1105/tpc.9.9.1621

Cited by 31 publications

(18 citation statements)

References 32 publications

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“…Therefore, the multiple proteins recognized by anti-LeGRP92 antibodies are encoded by the LeGRP92 gene. The mechanism that produces the four LeGRP92 forms is not known, but in the tapetum of Brassica oleracea, three transcripts are produced from the bopc3 gene (Ruiter et al 1997). The smaller transcripts are produced post-transcriptionally by deletions in the glycine-rich coding region of the mRNA.…”

Section: Discussionmentioning

confidence: 99%

“…Proposed functions for genes that are specifically expressed in the tapetum include lipid formation (Aarts et al 1997), lipid transport (Ross and Murphy 1996;Ruiter et al 1997), degradation of the callose wall (Hird et al 1993;Bucciaglia and Smith 1994), exine wall formation (Staiger et al 1994), pollen coat formation (Ross and Murphy 1996), production of allergens (de Dios Alché et al 1999), and pollen-stigma interaction (Zinkl et al 1999). Although a number of tapetal-specific genes have been identified, there has been little reported on the proteins they produce or their functions in pollen development.…”

Section: Introductionmentioning

confidence: 98%

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A glycine-rich protein that facilitates exine formation during tomato pollen development

McNeil

Smith

2009

Planta

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Formation of the unique and highly diverse outer cell wall, or exine, of pollen is essential for normal pollen function and survival. However, little is known about the many contributing proteins and processes involved in the formation of this wall. The tomato gene LeGRP92 encodes for a glycine-rich protein produced specifically in the tapetum. LeGRP92 is found as four major forms that accumulate differentially in protein extracts from stamens at different developmental stages. The three largest molecular weight forms accumulated during early microspore development, while the smallest molecular weight form of LeGRP92 was present in protein extracts from stamens from early microsporogenesis through anther dehiscence, and was the only form present in dehisced pollen. Light microscopy immunolocalization experiments detected LeGRP92 at only two stages, late tetrad and early free microspore. However, we observed accumulation of the LeGRP92 at the early tetrad stage of development by removing the callose wall from tetrads, which allowed LeGRP92 detection. Transmission electron microscopy confirmed the LeGRP92 accumulation from microspore mother cells, tetrads through anther dehiscence. It was observed in the callose surrounding the microspore mother cells and tetrads, the exine of microspores and mature pollen, and orbicules. Plants expressing antisense RNA had reduced levels of LeGRP92 mRNA and protein, which correlated to pollen with altered exine formation and reduced pollen viability and germination. These data suggest that the LeGRP92 has a role in facilitating sporopollenin deposition and uniform exine formation and pollen viability.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

A glycine-rich protein that facilitates exine formation during tomato pollen development

McNeil

Smith

2009

Planta

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“…Pollen coat proteins were separated by 12% SDS-PAGE and stained with Coomassie Brilliant Blue R250 or blotted onto a nitrocellulose membrane by electroblotting in 39 mM glycine, 48 mM Tris base, 0.037% (w/v) SDS, 20% (v/v) methanol, pH 8.3. The membranes were blocked overnight in blocking buffer (5% non-fat dried milk in PBT) and incubated with an antiserum raised against the total pollen coat proteins of Brassica oleracea (1:500 in blocking buffer; Ruiter et al 1997). After incubation with the primary antibody, membranes were rinsed and incubated with alkaline-phosphatase conjugated goat anti-rabbit antibody (Pierce, Rockford, Ill.; 1:20,000 in blocking buffer) for 1 h. The membranes were developed with 0.33 mg/ml nitro blue tetrazolium and 0.165 mg/ml 5-bromo-4-chloro-3-indolyl phosphatase in alkaline phosphatase buffer (100 mM Tris pH 9.5, 100 mM NaCl and 5 mM MgCl 2 ).…”

Section: Protein Isolation and Western Blottingmentioning

confidence: 99%

Oleosin-like proteins are not present on the surface of tobacco pollen

Bots¹,

Mariani²

2004

Sexual Plant Reproduction

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Pollen-stigma interactions on wet-and dry-type stigmas involve similar processes: the hydration of the pollen, followed by pollen tube growth and penetration of the stigma. Furthermore, in some species, identical molecules, namely lipids, are used to achieve this. In addition to lipids, oleosin-like proteins of the pollen coat of dry-type stigma plants have been shown to be involved in pollen-stigma interactions. However, little information is present about the proteins on the surface of pollen of wet-type stigma plants, in particular that of the Solanaceae. To analyze proteins from the surface of pollen of Nicotiana tabacum (tobacco), a solanaceous plant, we used an antiserum raised against Brassica pollen coat, a dry-type stigma plant of the Brassicaceae. In addition we used a molecular approach to identify tobacco homologues of oleosin-like genes. Our results show that no proteins similar to Brassica oleracea pollen coat proteins are present on the surface of tobacco pollen, and that oleosin-like genes are not expressed in tobacco anthers or stigmas.

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“…Sequence analysis was performed as described by Ruiter et al (1997a). Northern blot analysis was performed in accordance with Ruiter et al 1997b. Signals on blots were quantified by counting the radioactive spots in a liquid scintillation counter.…”

Section: Molecular Analysismentioning

confidence: 99%

“…The procedure was performed as described in Ruiter et al (1997b). Whole inflorescences were cut from the plant and left at room temperature to dry.…”

Section: Drought Stress Treatmentsmentioning

confidence: 99%

Hydration-dependent gene expression in Brassica oleracea anthers

Ruiter

Eldik

Herpen

et al. 1999

Sexual Plant Reproduction

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Anther physiology is characterized by developmentally controlled dehydration. Screening of an anther cDNA expression library with an antiserum raised against proteins isolated from the surface of Brassica oleracea pollen grains resulted in the isolation of bopc15 and bopc34, sequences similar to water stress-inducible genes. Bopc15 transcripts were exclusively present in pollen. The mRNA of bopc34 was found in various tissues, but not in pollen. The accumulation of both transcripts preceded anther dehydration. Premature anther dehydration induced by imposed drought stress affects gene expression in both the sporophytic and gametophytic portions of the anthers the levels of bopc15 and bopc34 transcripts increased to an extent dependent on developmental stage and duration of treatment. The inducible bopc15 transcript accumulation was reversible by rehydration. Bopc34 transcript levels, on the other hand, do not follow this pattern.

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Characterization of oleosins in the pollen coat of Brassica oleracea.

Cited by 31 publications

References 32 publications

A glycine-rich protein that facilitates exine formation during tomato pollen development

A glycine-rich protein that facilitates exine formation during tomato pollen development

Oleosin-like proteins are not present on the surface of tobacco pollen

Hydration-dependent gene expression in Brassica oleracea anthers

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