Involvement of the Golgi apparatus in crystalloid protein deposition in Ricinus communis cv. Hale seeds

1990 ◽  
Vol 68 (11) ◽  
pp. 2353-2360 ◽  
Author(s):  
M. J. Brown ◽  
J. S. Greenwood
Keyword(s):  
Storage Protein ◽  
Castor Bean ◽  
Protein Transport ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Protein Body ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
11S Globulin

The developing endosperm of castor bean has been used extensively as a model system for studies of storage-protein synthesis and processing, yet the path of transport of the storage proteins to the protein bodies has not been elucidated. In this study, immunolocalization of the 11S globulin (crystalloid protein) was performed on sections of acrolein–glutaraldehydefixed, resin-embedded, developing castor bean endosperm. Acrolein allowed rapid fixation of the tissue necessary for preserving the ultrastructure of the endomembrane system while maintaining adequate antigenicity of the target protein. Crystalloid protein was localized in the rough endoplasmic reticulum, the known site of synthesis, and in the dense proteinaceous inclusions within the protein bodies. In addition, significant labelling of Golgi complexes and associated vesicles, 65-nm diameter coated vesicles, and larger 220-nm diameter cytoplasmic vesicles was obtained. The findings provide the first direct evidence that the storage parenchyma cells of developing castor bean endosperm possess well-developed, functional Golgi complexes. This is consistent with previous observations of seed storage proteins in other plant species. The study further suggests that two distinct classes of vesicles are involved in the transport of the 11S globulin to the protein bodies. Key words: Golgi, immunolocalization, protein body, Ricinus communis, storage protein, transport (protein).

Seed storage proteins in cultivars and subspecies of alfalfa (Medicago sativa L.)

2000 ◽  
Vol 10 (4) ◽  
pp. 423-434 ◽  
Author(s):  
Joan E. Krochko ◽  
J. Derek Bewley
Keyword(s):  
Medicago Sativa ◽  
Storage Protein ◽  
Species Complex ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Patterns ◽  
2S Albumin ◽  
Two Dimensional Gel Electrophoresis ◽  
11S Globulin

AbstractSeed storage proteins were analysed in 27 varieties of alfalfa (Medicago sativaL.); these included five subspecies (glomerata, caerulea, falcata, hemicycla, praefalcata), seven of the nine sources of Medicago germplasm introduced into North America and a sample of additional cultivars. The protein patterns were remarkably consistent for all of these taxa. One-dimensional and two-dimensional gel electrophoresis revealed only minor differences in polypeptide composition within each of the three major classes of storage protein (7S globulin, 11S globulin, 2S albumin). The slight variations that were found provided no information on either parentage or evolutionary relationships amongst these particular taxa. Nonetheless, persistent and reproducible heterogeneity of some minor polypeptides of 11S globulin (medicagin) may be useful under other circumstances for cultivar identification in alfalfa. Both subfamilies (I and II) of the 11S globulin were strongly expressed in all of the cultivars and subspecies examined. It was concluded that this structural divergence within the 11S storage protein family predated the evolution of the M. sativa L. species complex. Most of the variability in storage proteins was quantitative. However, even this variability was reduced when data were standardized with respect to seed dry weights. The consistent similarities in qualitative and quantitative expression of seed storage proteins amongst all of these taxa suggest a high degree of uniformity in both seed physiology and genetics within the alfalfa species complex.

Seed development in Ricinus communis cv. Hale (castor bean). III. Pattern of storage protein and phytin accumulation in the endosperm

1985 ◽  
Vol 63 (12) ◽  
pp. 2121-2128 ◽  
Author(s):  
John S. Greenwood ◽  
J. Derek Bewley
Keyword(s):  
Seed Development ◽  
Storage Protein ◽  
Castor Bean ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Protein Body ◽  
Storage Organ ◽  
Endosperm Storage Protein ◽  
Reserve Accumulation ◽  
Cell Layers

The development of the endosperm of castor bean seed from its initial free nuclear state through to the end of maturation is presented. An investigation of the pattern of reserve accumulation in the endosperm at the light microscopy level revealed that the accumulation of soluble and insoluble storage proteins, and of phytin, does not occur simultaneously in all cells of the developing storage organ. Rates of reserve accumulation also vary among regions of the endosperm. Storage protein and phytin accumulation are initiated in a region midway between the periphery and central lumen of the endosperm by the early cotyledon stage of seed development. Afterwards, reserve deposition occurs more intensely in the proximal and more peripheral regions than in the distal and internal regions. A wave of reserve accumulation, or protein body maturation, proceeds from the more peripheral and the proximal regions to the more internal and distal regions as development continues. The last cells to complete reserve deposition are those in regions lying close to the endosperm lumen (into which the cotyledons have expanded) and the outermost two cell layers of the endosperm.

Pathways for protein transport to seed storage vacuoles

2005 ◽  
Vol 33 (5) ◽  
pp. 1016-1018 ◽  
Author(s):  
N.A. Jolliffe ◽  
C.P. Craddock ◽  
L. Frigerio
Keyword(s):  
Secretory Pathway ◽  
Protein Transport ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Seed Storage ◽  
Physical Structure ◽  
Working Model ◽  
Sorting Signals ◽  
Storage Vacuole

Plant vacuoles have multiple functions: they can act both as digestive organelles and as receptacles for storage proteins. Different types of vacuoles can coexist in the same cell, which adds complexity to the process of targeting to these compartments. A fuller understanding of this process is of evident value when endeavouring to exploit the plant secretory pathway for heterologous protein production. Positive sorting signals are required in order to sort proteins to vacuoles, and these have been split into three groups: ctVSS [C-terminal VSS (vacuolar sorting signals)], ssVSS (sequence-specific VSS) and physical structure VSS. The current working model posits that soluble proteins are delivered from the Golgi apparatus to the lytic vacuoles in clathrin-coated vesicles by virtue of their ssVSS, or to the storage vacuole [PSV (protein-storage vacuole)] in dense vesicles in a manner dependent on ctVSS or physical structure VSS. Although targeting to LV appears to be receptor-mediated, no such receptor has been identified for the recruitment of proteins to the PSV. We have studied the vacuolar targeting of two castor bean (Ricinus communis L.) storage proteins, proricin and pro 2 S albumin, in their native endosperm and in the heterologous system of tobacco protoplasts. We have found that both these proteins contain bona fide ssVSS and bind to sorting receptors in vitro in a similarly sequence-specific manner. The apparent similarities to lytic VSS and possible implications with respect to the working model for transport to storage vacuoles are discussed.

scholarly journals Amino Acid Sequencing and cDNA Cloning of Rice Seed Storage Proteins, the 13kDa Prolamins, Extracted from Type I Protein Bodies.

1999 ◽  
Vol 16 (2) ◽  
pp. 103-113 ◽  
Author(s):  
Norihiro MITSUKAWA ◽  
Ryoichi KONISHI ◽  
Kunitomo KIDZU ◽  
Kozo OHTSUKI ◽  
Takehiro MASUMURA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cdna Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
Type I ◽  
Rice Seed ◽  
Amino Acid Sequencing

Variability in the 11S globulin fraction of seed storage proteins ofHelianthus (Asteraceae)

1994 ◽  
Vol 193 (1-4) ◽  
pp. 69-79 ◽  
Author(s):  
Jacques Raymond ◽  
Brahim Mimouni ◽  
Jean-Louis Azanza
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Globulin Fraction ◽  
11S Globulin

Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame†

1999 ◽  
Vol 47 (12) ◽  
pp. 4932-4938 ◽  
Author(s):  
Sorgan S. K. Tai ◽  
Lawrence S. H. Wu ◽  
Emily C. F. Chen ◽  
Jason T. C. Tzen
Keyword(s):  
Molecular Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin ◽  
11S Globulin

scholarly journals Structural relationship between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) storage protein

1983 ◽  
Vol 213 (2) ◽  
pp. 543-545 ◽  
Author(s):  
S Odani ◽  
T Koide ◽  
T Ono ◽  
K Ohnishi
Keyword(s):  
Hordeum Vulgare ◽  
Trypsin Inhibitor ◽  
Sequence Homology ◽  
Storage Protein ◽  
Castor Bean ◽  
Storage Proteins ◽  
Proteinase Inhibitors ◽  
Ricinus Communis ◽  
Seed Proteins ◽  
Divergent Evolution

A significant sequence homology was found between barley (Hordeum vulgare) trypsin inhibitor and castor-bean (Ricinus communis) seed glutamine-rich storage protein. This appears to suggest a divergent evolution of the two different classes of seed proteins and to support a view that plant proteinase inhibitors may also act as storage proteins.

scholarly journals Evidence for a novel route of wheat storage proteins to vacuoles.

1992 ◽  
Vol 119 (5) ◽  
pp. 1117-1128 ◽  
Author(s):  
H Levanony ◽  
R Rubin ◽  
Y Altschuler ◽  
G Galili
Keyword(s):  
Golgi Complex ◽  
Protein Transport ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Wheat Seed ◽  
Considerable Part ◽  
Wheat Storage Protein ◽  
Wheat Storage Proteins ◽  
Electron Lucent

Wheat seed storage proteins are deposited in protein bodies (PB) inside vacuoles, but their subcellular site of aggregation and their route to vacuoles are still controversial. In the present work, an ultra structural analysis of developing wheat endosperm at early to mid maturation was performed to address these issues. Golgi complexes were rarely detected, indicating that their role in wheat storage protein transport is limited. In contrast, a considerable amount of PB was detected in the cytoplasm. Many of these PB were surrounded by RER membranes and were enlarged by fusion of smaller PB. Small, electron lucent vesicles were detected around the surfaces of the PB in the cytoplasm, or attached to them, suggesting that such attachments and subsequent fusion of the vesicles with each other lead to the formation of small vacuoles containing PB inclusions. Immunogold labeling with serum raised against yeast-BiP, an ER-localized protein, demonstrated that the wheat BiP homolog was present within the PB in the cytoplasm as well as inside vacuoles. This confirmed that the PB were formed within the RER and that the Golgi complex was not involved in their transport to vacuoles. It is concluded that a considerable part of the wheat storage proteins aggregate into PB within the RER and are then transported as intact PB to the vacuoles by a novel route that does not utilize the Golgi complex.

scholarly journals Assessment of Genetic Diversity in Bambara Groundnut (Vigna subterranea) Landraces Based on Seed Storage Proteins Electrophoretic Pattern

2021 ◽  
Vol 38 (1) ◽  
pp. 40-47
Author(s):  
N.M. Saminu ◽  
B.G. Kurfi ◽  
Y.Y. Muhammad
Keyword(s):  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Protein Profile ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Bambara Groundnut ◽  
Vigna Subterranea ◽  
Research Attention ◽  
Major Cluster

Bambara groundnut (Vigna subterranea) is a leguminous crop that is considered underutilized and has previously received little research attention. Variability in a number of physiological factors, including germination rate, widely affects its production. Seed storage protein, its fractions and protein profile of six Bambara groundnut local landraces were studied to assess their genetic relatedness. Total seed storage protein and its fractions were estimated by Bradford’s method. SDS-PAGE analysis was used to evaluate storage protein profile. The results showed significant differences (p<0.05) in protein contents among the landraces. The major seed storage proteins were found to be globulins (0.048 to 0.088mg/mL ), albumins (0.023 to 0.038mg/mL ), glutelins (0.007 to 0.013mg/mL ) and prolamins (0.002 to 0.004mg/mL ). Five peptide bands were detected with molecular weights corresponding to 97.4 kDa, 45 kDa, 29 kDa, 20.1 kDa and 18 kDa, respectively. Three peptide bands corresponding to 97.4 kDa, 45 kDa and 18 kDa were detected in all the landraces and two peptide bands between 29 kDa and 20.1 kDa were detected in five landraces. Dendrogram generated by UPGMA grouped the six landraces into one major cluster with two sub-clusters. The observed diversity in storage protein pattern of the landraces indicated their potential as materials for crop improvement.

Profiling the Seed Storage Protein Among Different Genotypes of Trigonella foenum-graecum L. (Fenugreek)

2019 ◽  
Author(s):  
Nisha . ◽  
Priyanka Khati ◽  
P B Rao
Keyword(s):  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Band ◽  
Trigonella Foenum Graecum ◽  
Trigonella Foenum Graecum L

A qualitative as well as quantitative categorization of seed storage proteins profiles of 23 genotypes of Trigonella foenum- graecum L. were performed by using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) for exploring the level of genetic discrepancy at seed storage protein level. Total soluble proteins were resolved on 10% resolving gel. A dendrogram was constructed on the basis of weight of seed storage proteins, which divide total genotypes into two groups further classified into different sub groups containing different genotypes in them. The bands obtained from gel electrophoresis can serve as a potent tool in discrimination of different genotypes on the basis of their protein content. Proteins with molecular weight 66, 43 and 35 kDa were found in all the genotypes except Fgk-76, PR, Rmt-303, PEB and Rmt-361, The 43 kDa protein band was found missing in Fgk-67, AFg-2, AM-2, AFg-4, Fgk-73, although the protein with 35 kDa weight was present in all the genotypes but not in Rmt-303 same as 63 kDa which is not present in Fgk-70 and 55 kDa protein band was found missing in Fgk-67, Afg-4 and Rmt-361.

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