Compartmentalization of seed reserve proteins

Adeli, Khosrow; Altosaar, Illimar

doi:10.1016/0014-5793(84)80599-2

Cited by 14 publications

(4 citation statements)

References 63 publications

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“…In any event, the different patterns of synthesis of PAPI, CI-1, and ASI make them model candidates for processing studies in aleurone cells. Studies on the intracellular deposition and/or secretion of these proteins might clarify the purported differences between endosperm and aleurone protein bodies (1,8,28).…”

Section: Discussionmentioning

confidence: 99%

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Differential Synthesis in Vitro of Barley Aleurone and Starchy Endosperm Proteins

Mundy¹,

Hejgaard²,

Hansen³

et al. 1986

Plant Physiol.

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To widen the selection of proteins for gene expression studies in barley seeds, experiments were performed to identify proteins whose synthesis is differentially regulated in developing and germinating seed tissues. The in vitro synthesis of nine distinct barley proteins was compared using mRNAs from isolated endosperm and aleurone tissues (developing and mature grain) and from cultured (germinating) aleurone layers treated with abscisic acid (ABA) and GA3. B and C hordein polypeptides and the salt-soluble proteins O-amylase, protein Z, protein C, the chymotrypsin inhibitors (CI-I and 2), the a-amylase/subtilisin inhibitor (ASI) and the inhibitor of animal cell-free protein synthesis systems (PSI) were synthesized with mRNA from developing starchy endosperm tissue. Of these proteins, f6-amylase, protein Z, and CI-1 and 2 were also synthesized with mRNA from developing aleurone cells, but ASI, PSI, and protein C were not. CI-I and also a probable amylase/protease inhibitor (PAPI) were synthesized at high levels with mRNAs from late developing and mature aleurone. These results show that mRNAs encoding PAPI and CI-I survive seed dessication and are long-lived in aleurone cells. Thus, expression of genes encoding ASI, PSI, protein C, and PAPI is tissue and stage-specific during seed development. Only ASI, CI-I, and PAPI were synthesized in significant amounts with mRNA from cultured aleurone layers. The levels of synthesis of PAPI and CI-1 were independent of hormone treatment. In contrast, synthesis of a-amylase (included as control) and of ASI showed antagonistic hormonal control: while GA promotes and ABA reduces accumulation of mRNA for a-amylase, these hormones have the opposite effect on ASI mRNA levels.One approach to understanding the molecular mechanisms controlling seed maturation and germination is to study organspecific, developmentally characteristic, and hormonally regulated seed proteins and their mRNAs. Earlier studies have identified such polypeptides in Gossypium (7) and Brassica (6) and have formed the basis of later work at the molecular level on these crops. We report here the results of similar experiments with barley seeds, a cereal of importance as livestock feed and as malt in the brewing industry.The barley seed or caryopsis is comprised of several tissues derived from the fertilized ovule (4). The seed proteins of the grain, synthesized during seed development in the endosperm and/or aleurone layer, include the hordeins (30-50% of total N, ' Present address:

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Section: Discussionmentioning

confidence: 99%

“…Electron microscopic studies have shown that the ultrastructure of protein bodies found in aleurone cells is different from those of starchy endosperm cells (for reviews see Refs. 1,28). Such differences imply differential expression during seed development of genes encoding various seed proteins in these two ontogenically closely related tissues.…”

mentioning

confidence: 99%

Differential Synthesis in Vitro of Barley Aleurone and Starchy Endosperm Proteins

Mundy¹,

Hejgaard²,

Hansen³

et al. 1986

Plant Physiol.

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“…All six datasets feature the characteristic starch metabolism, biosynthesis, and storage proteins. The content is affected by the starch preparation method used, as seed proteins have varying solubilities [ 37 ] and, as such, are divided into four solubility classes (the Osborne fractions): water-soluble albumins, water-insoluble globulins, alcohol-soluble gliadins, and insoluble glutenins [ 38 ]. As the first step of each method used imbibed and wet-ground rice, the albumins were solubilized and discarded early in the starch granule preparation.…”

Section: Discussionmentioning

confidence: 99%

Three Diverse Granule Preparation Methods for Proteomic Analysis of Mature Rice (Oryza sativa L.) Starch Grain

et al. 2022

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Starch is the primary form of reserve carbohydrate storage in plants. Rice (Oryza sativa L.) is a monocot whose reserve starch is organized into compounded structures within the amyloplast, rather than a simple starch grain (SG). The mechanism governing the assembly of the compound SG from polyhedral granules in apposition, however, remains unknown. To further characterize the proteome associated with these compounded structures, three distinct methods of starch granule preparation (dispersion, microsieve, and flotation) were performed. Phase separation of peptides (aqueous trypsin-shaving and isopropanol solubilization of residual peptides) isolated starch granule-associated proteins (SGAPs) from the distal proteome of the amyloplast and the proximal ‘amylome’ (the amyloplastic proteome), respectively. The term ‘distal proteome’ refers to SGAPs loosely tethered to the amyloplast, ones that can be rapidly proteolyzed, while proximal SGAPs are those found closer to the remnant amyloplast membrane fragments, perhaps embedded therein—ones that need isopropanol solvent to be removed from the mature organelle surface. These two rice starch-associated peptide samples were analyzed using nano-liquid chromatography–tandem mass spectrometry (Nano-HPLC-MS/MS). Known and novel proteins, as well as septum-like structure (SLS) proteins, in the mature rice SG were found. Data mining and gene ontology software were used to categorize these putative plastoskeletal components as a variety of structural elements, including actins, tubulins, tubulin-like proteins, and cementitious elements such as reticulata related-like (RER) proteins, tegument proteins, and lectins. Delineating the plastoskeletal proteome begins by understanding how each starch granule isolation procedure affects observed cytoplasmic and plastid proteins. The three methods described herein show how the technique used to isolate SGs differentially impacts the subsequent proteomic analysis and results obtained. It can thus be concluded that future investigations must make judicious decisions regarding the methodology used in extracting proteomic information from the compound starch granules being assessed, since different methods are shown to yield contrasting results herein. Data are available via ProteomeXchange with identifier PXD032314.

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“…Similarly, plant biotechnology takes advantage of the storage and delivery properties of proteins bodies by using specific promoters to target cytokines, vaccine candidates, growth hormones and other biopharmaceuticals to the seed endosperm, a natural protein deposition site (Adeli & Altosaar, 1984;Wright et al, 2001;Sardana et al, 2002). In this study, we explored the accumulation of rhCD14 protein in transgenic tobacco seeds.…”

Section: Introductionmentioning

confidence: 97%

Human CD14 Expressed in Seeds of Transgenic Tobacco Displays Similar Proteolytic Resistance and Bioactivity with its Mammalian-produced Counterpart

Blais

Altosaar

2006

Transgenic Res

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Human CD14 plays an important role in innate immunity by being the key receptor of lipopolysaccharide found on Gram-negative bacteria. The recently discovered widespread localization of CD14 in secretions and mucosal surfaces reveals its extensive anti-microbial properties and numerous potential medical applications. To produce active recombinant human CD14 (rhCD14) for massive distribution, transgenic tobacco plants were successfully generated to express rhCD14 in the seed endosperm under the control of two versions (1.8 kb and 5.1 kb) of the rice glutelin Gt-1 promoter. Plant-made rhCD14 proteins reached a concentration of 16 microg/g of seeds and showed stability, proteolytic resistance to pepsin digestion and ability to induce the release of pro-inflammatory IL-6 and IL-8 cytokines in presence of LPS. The expression of plant rhCD14 in tobacco seeds constitutes a promising low-cost and abundant supply of this immune protein to further investigate its roles in, impacts on and potential medical applications for the innate immune system.

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Compartmentalization of seed reserve proteins

Cited by 14 publications

References 63 publications

Differential Synthesis in Vitro of Barley Aleurone and Starchy Endosperm Proteins

Differential Synthesis in Vitro of Barley Aleurone and Starchy Endosperm Proteins

Three Diverse Granule Preparation Methods for Proteomic Analysis of Mature Rice (Oryza sativa L.) Starch Grain

Human CD14 Expressed in Seeds of Transgenic Tobacco Displays Similar Proteolytic Resistance and Bioactivity with its Mammalian-produced Counterpart

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