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 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 ◽  
Author(s):  
Ren-shui LIU ◽  
Guo-qing WEI ◽  
Qiang YANG ◽  
Wen-jun HE ◽  
Wang-Yi LIU
Keyword(s):  
Storage Protein ◽  
Cinnamomum Camphora ◽  
Type Ii ◽  
Ribosome Inactivating Protein ◽  
Camphor Tree

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).

The physiological role of storage proteins in seeds

1984 ◽  
Vol 304 (1120) ◽  
pp. 275-285 ◽  
Keyword(s):  
Storage Protein ◽  
Protein Fraction ◽  
Storage Proteins ◽  
Physiological Role ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nutrient Deficiencies ◽  
Cellular Mechanisms ◽  
Post Translational Modifications ◽  
Developing Seed

Seed storage proteins provide a source of amino acids and reduced N necessary for germination and early growth of the seedling. Because the long term aim of much of the current research in this area is to modify the composition of the storage protein fraction, it is of interest to ask w hat kinds of changes might be tolerated by the developing seed without affecting this physiological role. For example, glycosylation and many of the post-translational modifications seen in some legume storage proteins may not be essential and major alterations in the relative amounts of the component proteins in the storage protein fraction are also tolerated. Some nutrient deficiencies result in very extensive changes in this latter category and nutrient deficient plants provide a useful tool for the study of some of the cellular mechanisms that regulate the composition of the storage protein fraction. Sulphur deficiency and potassium deficiency have contrasting effects on the relative proportions of legumin and vicilin in pea seeds. These changes are mainly the result of altered levels of their respective mRNAs together with a change in the pattern of synthesis and accumulation of these two proteins during seed development.

Cinnamomin—a Versatile Type II Ribosome-inactivating Protein

2004 ◽  
Vol 36 (3) ◽  
pp. 169-176 ◽  
Author(s):  
Hong Xu ◽  
Wang-Yi Liu
Keyword(s):  
Theoretical Study ◽  
Physiological Role ◽  
Type Ii ◽  
Insect Larvae ◽  
Ribosome Inactivating Protein ◽  
Ribosome Inactivating Proteins ◽  
Enzymatic Mechanism ◽  
Potential Applications ◽  
And Function ◽  
Mature Seeds

Abstract Ribosome-inactivating proteins (RIPs) are a group of toxic proteins that can specifically act on the universally conserved sarcin/ricin domain (S/R domain) of the largest RNA in ribosome and thus irreversibly inactivate ribosome for protein synthesis. Cinnamomin is a multifunctional type II RIP isolated in our laboratory from the mature seeds of the camphor tree. This protein has been extensively studied with regard to its purification, characteristics, structure and function, genetic expression, enzymatic mechanism, physiological role in seed cell and toxicity to cancer cells and insect larvae. The research results of cinnamomin obtained in our laboratory are summarized in this review. Understanding of cinnamomin and the relative new proteins will help expand our knowledge of RIPs and may accelerate theoretical study and the development of their potential applications.

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.

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 Molecular linkage map of Einkorn wheat: mapping of storage-protein and soft-glume genes and bread-making quality QTLs

2002 ◽  
Vol 80 (2) ◽  
pp. 131-143 ◽  
Author(s):  
B. TAENZLER ◽  
R. F. ESPOSTI ◽  
P. VACCINO ◽  
A. BRANDOLINI ◽  
S. EFFGEN ◽  
...  
Keyword(s):  
Protein Content ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Proteins ◽  
Total Protein Content ◽  
Protein Markers ◽  
Bread Making ◽  
Einkorn Wheat ◽  
Significant Qtls ◽  
Sedimentation Volume

Two molecular maps of Triticum monococcum L were produced and integrated. The integrated map includes a total of 477 markers, 32 RFLPs, 438 AFLPs, one morphological (soft glume (Sog)) and six storage-protein markers, and covers 856 cM. The trait Sog with the recessive allele sog maps to linkage group 2S. Probably, this is the T. monococcum homologue of Tg and Tg2 in hexaploid and tetraploid wheats, respectively. Loci coding for seed storage proteins were allocated to chromosomes 1L (HMW GLU1,2 and Glu1), 1S (LMW GLU6,7, LMW GLU1-4, ωGLI1-4, γGLI5 and Gli-1) and 6L (α/βGLI7-14). Parameters related to bread-making quality (SDS sedimentation volume, specific sedimentation volume (SSV) and total protein content) were studied in one of the two populations. A QTL that is consistently present across environments was detected for SDS sedimentation volume and for SSV. The position of the QTL on chromosome 1S was in close agreement with the map positions of storage-protein loci. A second QTL was mapped on chromosome 5. For protein content, two significant QTLs were mapped to linkage groups 1 and 5.

scholarly journals Genetic variation in common bean (Phaseolus vulgaris L.) using seed protein markers

2020 ◽  
Vol 12 (1) ◽  
pp. 58-69
Author(s):  
Henok Ayelign ◽  
Eleni Shiferaw ◽  
Faris Hailu
Keyword(s):  
Common Bean ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Gene Diversity ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Markers ◽  
Mesoamerican Gene Pool

AbstractThe genetic diversity of common bean accessions were assessed using seed storage protein markers. At regional level, accessions from the two major growing regions showed the highest level of gene diversity (H = 0.322, I = 0.485, and H = 0.312, I = 0.473), which can be exploited for the future improvement of the crop. Based on phaseolin, the major storage protein in common bean, the majority of the accessions (86%) were grouped under Mesoamerican gene pool. Seed proteins were also used to differentiate various Phaseolus species, indicating the usefulness of seed storage proteins in species identification in this genus.

scholarly journals Identification and Characterization of the Seed Storage Proteins and Related Genes of Cannabis sativa L.

2021 ◽  
Vol 8 ◽  
Author(s):  
Xin Sun ◽  
Yao Sun ◽  
Yao Li ◽  
Qiong Wu ◽  
Lei Wang
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Storage Protein ◽  
Cannabis Sativa ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Hemp Seed ◽  
Abundant Protein ◽  
Molecular Weights

Hemp (Cannabis sativa L.) seed is emerging as a novel source of plant protein owing to its rich protein content and reasonable nutritional structure. In the current study, the storage proteins of hemp seed were extracted using different methods. The modified Osborne method yielded maximum extraction of the hemp seed storage proteins, while degreasing had little effect on the hemp seed protein (HSP) extraction. Protein identification results revealed that 11S globulin (edestin) was the most abundant protein in hemp seed, and the molecular weights of the two subunits of this protein were ~35 and 20 kDa, respectively. The second most abundant protein was 2S albumin (Cs2S), with a molecular weight of ~14–15 kDa. The least abundant protein was 7S vicilin-like protein (Cs7S), with a molecular weight of ~47 kDa. Subsequently, gene families encoding these three storage protein classes, including three genes for edestin, two for Cs2S, and one for Cs7S, were cloned and then analyzed for amino acid composition and structure. The three edestins were different in their amino acid sequences and calculated molecular weights. The analysis of coding sequences revealed a higher percentage of similarity (62.7%) between Edestin1 and Edestin3, while the similarity decreased significantly to ~57% between Edestin1 and Edestin2, and 58% between Edestin2 and Edestin3. The calculated protein molecular weight was the highest for the protein encoded by Edestin1 and the smallest for the protein encoded by Edestin2. All three edestins were rich in arginine, while Edestin3 had a higher methionine content relative to that in the other two, which proved that Edestin3 had a better nutritional value. Cs2S and Cs7S were different from those reported in previous studies. Therefore, it could be inferred that amino acid composition varies with different hemp cultivars. The current research brought significant theoretical advance in illuminating the understanding of hemp seed storage protein and would have significance for future research on improving the nutritional quality of hemp seed and developing bioactive peptides.

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.

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