Soybean vegetative lipoxygenases are not vacuolar storage proteins

2011 ◽  
Vol 38 (10) ◽  
pp. 778 ◽  
Author(s):  
Glenn W. Turner ◽  
Howard D. Grimes ◽  
B. Markus Lange
Keyword(s):  
Storage Proteins ◽  
Tissue Level ◽  
Protein Bodies ◽  
Specific Antibodies ◽  
Vegetative Storage Proteins ◽  
Paraveinal Mesophyll ◽  
Cast Doubt ◽  
Sink Limitation ◽  
Immuno Cytochemistry

The paraveinal mesophyll (PVM) of soybean is a distinctive uniseriate layer of branched cells situated between the spongy and palisade chlorenchyma of leaves that contains an abundance of putative vegetative storage proteins, Vspα and Vspβ, in its vacuoles. Soybean vegetative lipoxygenases (five isozymes designated as Vlx(A–E)) have been reported to co-localise with Vsp in PVM vacuoles; however, conflicting results regarding the tissue-level and subcellular localisations of specific Vlx isozymes have been reported. We employed immuno-cytochemistry with affinity-purified, isozyme-specific antibodies to reinvestigate the subcellular locations of soybean Vlx isozymes during a sink limitation experiment. VlxB and VlxC were localised to the cytoplasm and nucleoplasm of PVM cells, whereas VlxD was present in the cytoplasm and nucleoplasm of mesophyll chlorenchyma (MC) cells. Label was not associated with storage vacuoles or any evident protein bodies, so our results cast doubt on the hypothesis that Vlx isozymes function as vegetative storage proteins.

The functional status of paraveinal mesophyll vacuoles changes in response to altered metabolic conditions in soybean leaves

2005 ◽  
Vol 32 (4) ◽  
pp. 335 ◽  
Author(s):  
Kimberly A. Murphy ◽  
Rachel A. Kuhle ◽  
Andreas M. Fischer ◽  
Aldwin M. Anterola ◽  
Howard D. Grimes
Keyword(s):  
Functional Status ◽  
Storage Proteins ◽  
Vegetative Storage Proteins ◽  
Paraveinal Mesophyll ◽  
Lytic Function ◽  
Metabolic Conditions ◽  
Glycine Max L ◽  
Soybean Leaves ◽  
And Storage ◽  
Lytic Compartment

Antibodies raised against tonoplast intrinsic proteins (TIPs) were used to probe the functional status of the soybean [Glycine max (L.) Merr.] paraveinal mesophyll (PVM) vacuole during changes in nitrogen metabolism within the leaf. Young plants grown under standard conditions had PVM vacuoles characterised by the presence of γ-TIP, which is indicative of a lytic function. When plants were then subjected to shoot tip removal for a period of 15 d, forcing a sink-limited physiological condition, the γ-TIP marker diminished while the δ-TIP marker became present in the PVM vacuole, indicating the conversion of the PVM vacuole to a storage function. When the shoot tips were allowed to regrow, the γ-TIP marker again became dominant demonstrating the reversion of these PVM vacuoles back to a lytic compartment. The changes in TIP markers correlated with the accumulation of vegetative storage proteins and vegetative lipoxygenases, proteins implicated in nitrogen storage and assimilate partitioning. This research suggests that the PVM vacuole is able to undergo dynamic conversion between lytic and storage functions and further implicates this cell layer in assimilate storage and mobilisation in soybeans.

Cotyledonary Storage Proteins in Pisum sativum. IV. Effects of Sulfur, Phosphorus, Potassium and Magnesium Deficiencies

1979 ◽  
Vol 6 (1) ◽  
pp. 11 ◽  
Author(s):  
PJ Randall ◽  
JA Thomson ◽  
HE Schroeder
Keyword(s):  
Storage Proteins ◽  
Nutrient Deficiency ◽  
Fold Increase ◽  
Insoluble Fraction ◽  
Mineral Elements ◽  
Relative Increase ◽  
Protein Bodies ◽  
Total N ◽  
S Deficiency ◽  
Plant Yields

The quantitative and qualitative effects of deficiency of S, P, K or Mg on the cotyledonary proteins of pea seeds have been studied using chemical, immunological and electrophoretic techniques. Deficiency of S, P or K causes characteristic and consistent changes in the proportions of certain proteins both outside and inside protein bodies of mature seeds. Amongst the storage proteins in the protein bodies, S deficiency results in a relative decrease in legumin and in vicilin peak 3, accompanied by a relative increase in the predominant vicilin, peak 4. A quantitatively major cotyledonary protein of unknown function, located outside protein bodies and consisting of 22- kdalton polypeptides, is decreased by S deficiency. Deficiencies of P or K cause an increase in the quantitatively minor vicilin peak 3 and also a marked relative increase in legumin. Mg deficiency has little effect on the proportions of the storage proteins. The degree of nutrient deficiency is reflected in seed and plant yields. Total N and trichloroacetic acid (TCA)-insoluble N and the contents of some other mineral elements in the seed are given. A 10-fold increase in sulfur supply above the optimum for yield did not increase N or S in the TCA- insoluble fraction.

Cruciferous Oilseed Proteins: the Protein Bodies of Sinapis alba Seed

1976 ◽  
Vol 3 (6) ◽  
pp. 731 ◽  
Author(s):  
JTO Kirk ◽  
NA Pyliotis
Keyword(s):  
Proteolytic Activity ◽  
Storage Proteins ◽  
Protein Body ◽  
Protein Bodies ◽  
Seed Meal ◽  
Mustard Seed ◽  
Major Protein ◽  
Intense Band ◽  
Ungerminated Seed ◽  
Protein Classes

The solubility properties of the proteins of oil-free meal of white mustard seed (S. alba) in various aqueous extraction media are described. Electrophoresis on cellulose acetate of a salt extract of the seed meal at pH 7.0 shows the presence of two positively charged protein bands: a slow moving intense band (I) and a less intense band with higher mobility (II). On the basis of Sephadex G100 chromatography and sedimentation behaviour, these bands are deemed to be identical with the two major protein classes (12 S and 1.7 S, respectively) present in this and other Brassica-related species, as described by other workers. Centrifugation after filtration of a seed meal homogenate yields a preparation that is completely soluble in salt solution, and can be shown by electron microscopy to consist entirely of protein body fragments. Only the 12 S protein can be detected in significant quantity in this preparation: this protein at least we may assume to be present in the aleurone (protein) grains observed in micrographs of the cotyledon cells. In germinating seeds, disappearance of protein bodies is accompanied by a diminution in total salt-soluble protein and in the amounts of the 12 S and 1.7 S proteins, supporting their identification as storage proteins. The rate of utilization is the same in the light and in the dark. Proteolytic activity was detected in the ungerminated seed. The level of activity was more than sufficient to account for the subsequent observed rate of protein utilization. Proteolytic activity per seed increased by only 40-70% during 4 days germination.

Characterization of storage proteins extracted from Avena sativa seed protein bodies

1982 ◽  
Vol 30 (1) ◽  
pp. 32-36 ◽  
Author(s):  
Jean Claude Pernollet ◽  
Su Il Kim ◽  
Jacques Mosse
Keyword(s):  
Avena Sativa ◽  
Seed Protein ◽  
Storage Proteins ◽  
Protein Bodies

DISTRIBUTION OF VEGETATIVE STORAGE PROTEINS IN ROSACEAE

IAWA Journal ◽  
2003 ◽  
Vol 24 (4) ◽  
pp. 421-428
Author(s):  
Wei-Min Tian ◽  
Zheng-Hai Hu
Keyword(s):  
Seasonal Changes ◽  
Storage Proteins ◽  
Protein Body ◽  
Diagnostic Feature ◽  
Secondary Phloem ◽  
Apple Trees ◽  
Phloem Parenchyma ◽  
Vegetative Storage Proteins ◽  
Parenchyma Cells ◽  
First Time

The distribution pattern of vegetative storage proteins is reported for the first time for 18 species and 2 varieties of twelve genera of Rosaceae. Vegetative storage proteins were present in all the species studied of Prunoideae and absent in Maloideae. Their occurrence in a genus seemed to be either universal or entirely absent. Rosaceae trees were poor in vegetative storage proteins and the form of vegetative storage proteins was not protein body-like. Granular and floccular forms of vegetative storage proteins could be distinguished exclusively in the secondary phloem parenchyma cells and their distribution was cell-specific. Our results suggest that the distribution of vegetative storage proteins in Rosaceae can be considered as a taxonomically diagnostic feature. The nature of the bark proteins with seasonal changes in apple trees is discussed.

Root storage proteins, with particular reference to taproots

2002 ◽  
Vol 80 (4) ◽  
pp. 321-329 ◽  
Author(s):  
J Derek Bewley
Keyword(s):  
Total Nitrogen ◽  
Storage Proteins ◽  
Minor Component ◽  
Early Summer ◽  
Crop Species ◽  
Nitrogen Pool ◽  
Vegetative Storage Proteins ◽  
Perennial Weeds ◽  
Nitrogen Pools ◽  
Root Proteins

The presence of storage proteins has been reported in roots of several perennial and biennial weed and crop species, and particularly in members of the Compositae, Euphorbiaceae, and Leguminosae. In some species the amount of these root proteins fluctuates seasonally, increasing in the fall and winter months and declining in the spring and early summer. Also, the root proteins may decline during regrowth of decapitated plants. The evidence that these proteins play a role as storage proteins is frequently only circumstantial; moreover, they are usually only a relatively minor component of the total nitrogen pool within the root. Only one root protein, that from the dandelion taproot, has been extensively characterized, and it has no properties in common with known vegetative storage proteins. The literature on root proteins is reviewed, with particular emphasis on those present in taproots. The paucity of definitive data allows few conclusions to be reached, and more research is required to establish the role, nature, and importance of root proteins.Key words: taproots, perennial weeds, root proteins, nitrogen pools, storage proteins.

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