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.

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).

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 The Role of RNA-Binding Protein OsTudor-SN in Post-Transcriptional Regulation of Seed Storage Proteins and Endosperm Development

2019 ◽  
Vol 60 (10) ◽  
pp. 2193-2205
Author(s):  
Hong-Li Chou ◽  
Li Tian ◽  
Masako Fukuda ◽  
Toshihiro Kumamaru ◽  
Thomas W Okita
Keyword(s):  
Protein Expression ◽  
Seed Development ◽  
Storage Protein ◽  
Rna Binding ◽  
Storage Proteins ◽  
Protein Body ◽  
Grain Weight ◽  
Protein Accumulation ◽  
Body Type ◽  
Body Formation

Abstract Tudor-SN is involved in a myriad of transcriptional and post-transcriptional processes due to its modular structure consisting of 4 tandem SN domains (4SN module) and C-terminal Tsn module consisting of Tudor-partial SN domains. We had previously demonstrated that OsTudor-SN is a key player for transporting storage protein mRNAs to specific ER subdomains in developing rice endosperm. Here, we provide genetic evidence that this multifunctional RBP is required for storage protein expression, seed development and protein body formation. The rice EM1084 line, possessing a nonsynonymous mutation in the 4SN module (SN3 domain), exhibited a strong reduction in grain weight and storage protein accumulation, while a mutation in the Tudor domain (47M) or the loss of the Tsn module (43M) had much smaller effects. Immunoelectron microscopic analysis showed the presence of a new protein body type containing glutelin and prolamine inclusions in EM1084, while 43M and 47M exhibited structurally modified prolamine and glutelin protein bodies. Transcriptome analysis indicates that OsTudor-SN also functions in regulating gene expression of transcriptional factors and genes involved in developmental processes and stress responses as well as for storage proteins. Normal protein body formation, grain weight and expression of many genes were partially restored in EM1084 transgenic line complemented with wild-type OsTudor-SN gene. Overall, our study showed that OsTudor-SN possesses multiple functional properties in rice storage protein expression and seed development and that the 4SN and Tsn modules have unique roles in these processes.

scholarly journals cDNA-AFLP analysis of transcript derived fragments during seed development in castor bean (Ricinus communis L.)

2018 ◽  
Vol 32 (5) ◽  
pp. 1119-1125 ◽  
Author(s):  
Fenglan Huang ◽  
Mu Peng ◽  
Xiaofeng Chen ◽  
Guorui Li ◽  
Jianjun Di ◽  
...  
Keyword(s):  
Seed Development ◽  
Castor Bean ◽  
Ricinus Communis ◽  
Aflp Analysis ◽  
Ricinus Communis L

scholarly journals Immunolocalization of ricin accumulation during castor bean (Ricinus communis L.) seed development

2010 ◽  
Vol 1 (2) ◽  
pp. 12 ◽  
Author(s):  
Aisy Botega Baldoni ◽  
Ana Cláudia Guerra Araújo ◽  
Mayara Holanda De Carvalho ◽  
Ana Cristina M. M. Gomes ◽  
Francisco J. L. Aragao
Keyword(s):  
Seed Development ◽  
Castor Bean ◽  
Ricinus Communis ◽  
Cellular Level ◽  
Ultrastructural Changes ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Ricinus Communis L ◽  
The Matrix ◽  
Localization Signal

Ricin is a dimeric glycoprotein that accumulates in protein storage vacuoles of endosperm cells of Ricinus communis L. (castor bean). The proricin travels through the Golgi appar­atus and co-localizes throughout its route to the storage vacuoles of developing castor bean endosperm. We report here the pattern of seed morphological and ultrastructural changes during various stages of seed development, associated with ricin accumulation. ELISA was used to compare the ricin content in mature seeds of four Brazilian commercial cultivars. ELISA and immunoelectron microscopy anal­ysis were used to study ricin accumulation during seed development from 10 to 60 days after pollination (DAP). Results have shown that no ricin could be localized in the endosperm cells in the early development stages (before 20 DAP) and only a few localization points could be observed at 30 DAP. However, a significant ricin localization signal was observed at 40 DAP in the matrix of the protein storage vacuoles. The signal increased significantly from 50 to 60 DAP, when ricin was observed in both the matrix and crystalloids of the protein storage vacuoles. Understanding ricin expression at the cellular level is fundamental for the development of strategies for gene suppression using molecular breeding approaches.

scholarly journals Identification and expression analysis of a novel phytocystatin in developing and germinating seeds of triticale (×Triticosecale Wittm.)

2015 ◽  
Vol 84 (1) ◽  
pp. 139-142 ◽  
Author(s):  
Joanna Simińska ◽  
Wiesław Bielawski
Keyword(s):  
Seed Germination ◽  
Seed Development ◽  
Storage Protein ◽  
Cdna Sequence ◽  
Storage Proteins ◽  
Cysteine Proteinase ◽  
Protein Accumulation ◽  
Protein Levels ◽  
Germinating Seeds ◽  
Cysteine Proteinase Activity

In this paper the complete cDNA sequence of a newly identified triticale phytocystatin, TrcC-7, was analyzed. Because <em>TrcC-7</em> transcripts were present in seeds, we hypothesized that it may regulate storage protein accumulation and degradation. Therefore, changes in mRNA and protein levels during the entire period of seed development and germination were examined. Expression of <em>TrcC-7</em> increased during development and decreased at the end of maturation and subsequently increased during seed germination. Based on these results, TrcC-7 likely regulates cysteine proteinase activity during the accumulation and mobilization of storage proteins.

Cinnamomin, a type II ribosome-inactivating protein, is a storage protein in the seed of the camphor tree (Cinnamomum camphora)

2002 ◽  
Vol 362 (3) ◽  
pp. 659-663 ◽  
Author(s):  
Ren-shui LIU ◽  
Guo-qing WEI ◽  
Qiang YANG ◽  
Wen-jun HE ◽  
Wang-Yi LIU
Keyword(s):  
Western Blotting ◽  
Storage Protein ◽  
Storage Proteins ◽  
Protein Body ◽  
Physiological Role ◽  
Seed Storage Proteins ◽  
Cinnamomum Camphora ◽  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
Camphor Tree

Cinnamomin is a novel type II ribosome-inactivating protein (RIP) isolated in our laboratory from the seed of the camphor tree (Cinnamomum camphora). In this paper the physiological role it plays in the plant cell was studied. Northern and Western blotting revealed that cinnamomin was expressed specifically in cotyledons. It accumulated in large amounts simultaneously with other proteins at the post-stages of seed development. Cinnamomin degraded rapidly during the early stages of seed germination. Endopeptidase was proved to play an important role in the degradation of cinnamomin. Western blotting of total proteins from the protein body with antibodies against cinnamomin demonstrated that it only existed in this specific cellular organelle as a storage protein. The similar properties of cinnamomin and other seed storage proteins of dicotyledons were compared. We conclude that cinnamomin is a special storage protein in the seed of C. camphora.

scholarly journals Genomic Characterization and Expressional Profiles of Autophagy-Related Genes (ATGs) in Oilseed Crop Castor Bean (Ricinus communis L.)

2020 ◽  
Vol 21 (2) ◽  
pp. 562 ◽  
Author(s):  
Bing Han ◽  
Hui Xu ◽  
Yingting Feng ◽  
Wei Xu ◽  
Qinghua Cui ◽  
...  
Keyword(s):  
Potential Function ◽  
Seed Development ◽  
Seed Coat ◽  
Castor Bean ◽  
Lipid Droplets ◽  
Ricinus Communis ◽  
Expression Patterns ◽  
Oilseed Crop ◽  
Seed Biology ◽  
Cellular Autophagy

Cellular autophagy is a widely-occurring conserved process for turning over damaged organelles or recycling cytoplasmic contents in cells. Although autophagy-related genes (ATGs) have been broadly identified from many plants, little is known about the potential function of autophagy in mediating plant growth and development, particularly in recycling cytoplasmic contents during seed development and germination. Castor bean (Ricinus communis) is one of the most important inedible oilseed crops. Its mature seed has a persistent and large endosperm with a hard and lignified seed coat, and is considered a model system for studying seed biology. Here, a total of 34 RcATG genes were identified in the castor bean genome and their sequence structures were characterized. The expressional profiles of these RcATGs were examined using RNA-seq and real-time PCR in a variety of tissues. In particular, we found that most RcATGs were significantly up-regulated in the later stage of seed coat development, tightly associated with the lignification of cell wall tissues. During seed germination, the expression patterns of most RcATGs were associated with the decomposition of storage oils. Furthermore, we observed by electron microscopy that the lipid droplets were directly swallowed by the vacuoles, suggesting that autophagy directly participates in mediating the decomposition of lipid droplets via the microlipophagy pathway in germinating castor bean seeds. This study provides novel insights into understanding the potential function of autophagy in mediating seed development and germination.

scholarly journals Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.)

1985 ◽  
Vol 225 (1) ◽  
pp. 239-247 ◽  
Author(s):  
J A Gatehouse ◽  
J Gilroy ◽  
M S Hoque ◽  
R R D Croy
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Amino Acid Sequence ◽  
Storage Protein ◽  
Seed Protein ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Pisum Sativum L ◽  
New Type ◽  
Pea Seeds

The seeds of pea (Pisum sativum L.) contain several proteins in the albumin solubility fraction that are significant components of total cotyledonary protein (5-10%) and are accumulated in developing seeds concurrently with storage-protein synthesis. One of these proteins, of low Mr and designated ‘Psa LA’, has been purified, characterized and sequenced. Psa LA has an Mr of 11000 and contains polypeptides of Mr 6000, suggesting that the protein molecules are dimeric. The amino acid sequence contains 54 residues, with a high content (10/54) of asparagine/aspartate. It has no inhibitory action towards trypsin or chymotrypsin, and is distinct from the inhibitors of those enzymes found in pea seeds, nor does it inhibit hog pancreatic alpha-amylase. The protein contains no methionine, but significant amounts of cysteine (four residues per polypeptide), suggesting a possible role as a sulphur storage protein. However, its sequence is not homologous with low-Mr (2S) storage proteins from castor bean (Ricinus communis) or rape (Brassica napus). Psa LA therefore represents a new type of low-Mr seed protein.

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