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 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.

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.

Control of storage protein accumulation during legume seed development

2001 ◽  
Vol 158 (4) ◽  
pp. 457-464 ◽  
Author(s):  
Sabine Golombek ◽  
Hardy Rolletschek ◽  
Ulrich Wobus ◽  
Hans Weber
Keyword(s):  
Seed Development ◽  
Storage Protein ◽  
Protein Accumulation ◽  
Legume Seed

Vegetative storage protein expression during terminal bud formation in poplar

2001 ◽  
Vol 31 (6) ◽  
pp. 1098-1103 ◽  
Author(s):  
Susan D Lawrence ◽  
Janice EK Cooke ◽  
John S Greenwood ◽  
Theresa E Korhnak ◽  
John M Davis
Keyword(s):  
Protein Expression ◽  
Shoot Apex ◽  
Storage Protein ◽  
Messenger Rna ◽  
Storage Proteins ◽  
N Cycling ◽  
Mrna Levels ◽  
Vegetative Storage Protein ◽  
Bud Formation ◽  
Terminal Bud

Trees recycle nitrogen (N) to conserve this valuable nutrient. The processes that regulate N recycling within trees are poorly understood at the molecular level. Because vegetative storage proteins (VSPs) are thought to play important roles in within-plant N cycling, we are investigating the expression of VSP genes to gain insights into how seasonally controlled N cycling is regulated in trees. We compared steady-state mRNA levels of three different VSP homologs during short day induced terminal bud formation in hybrid poplar (Populus trichocarpa Torr. & Gray × Populus deltoides Bartr. ex Marsh.) – WIN4 (wound-inducible protein 4), BSP (bark storage protein), and pni288 (poplar nitrogen-regulated cDNA 288, a newly identified sequence). We determined that win4 and pni288 transcripts decrease, while bsp transcripts increase, as the terminal bud is formed. Immunolocalization analysis indicated that, during apical bud formation, BSP accumulates in the ground meristem and in parenchyma cells adjacent to xylem and proximal to the apical dome. Based on messenger RNA and protein expression analysis, we conclude that different VSPs play distinct roles in the poplar shoot apex, with BSP accumulating as a reserve near the shoot apex during terminal bud formation.

Structural Aspects of Protein Accumulation in Developing Pea Cotyledons. III. Immunocytochemical Localization of Legumin and Vicilin Using Antibodies Shown to Be Specific by the Enzyme-Linked Immunosorbent Assay (ELISA)

1980 ◽  
Vol 7 (3) ◽  
pp. 339 ◽  
Author(s):  
S Craig ◽  
A Millerd ◽  
DJ Goodchild
Keyword(s):  
Immunosorbent Assay ◽  
Storage Proteins ◽  
Protein Body ◽  
Protein Bodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Accumulation ◽  
Immunocytochemical Localization ◽  
Elisa Technique ◽  
Immunocytochemical Techniques ◽  
Structural Aspects

The site of sequestration of the storage proteins legumin and vicilin during development of cotyledons from pea (Pisum sativum L.) has been determined using improved immunocytochemical techniques. Antibodies to legumin and vicilin were made monospecific by affinity chromatography. They were allowed to react on sections of glycol methacrylate-embedded cotyledon tissue and detected by indirect immunocytochemical localization using rhodamine-labelled antibodies. The enzyme-linked immunosorbent assay (ELISA) technique was adapted to verify antibody specificity at a sensitivity up to 300 times greater than that of immunodiffusion. Legumin and vicilin 4 are localized in small peripheral deposits within large vacuoles as early as day 8 after flowering. As the vacuoles fragment during development the storage proteins continue to be localized in the vacuolar deposits until, at day 16, they entirely fill vacuoles, now termed protein bodies. Thereafter, the protein bodies become more densely packed and retain a similar form from day 22 to maturity. Wherever the same vacuolar deposit of protein body could be observed in adjacent sections, antilegumin and antivicilin 4 labelled both deposits, clearly indicating that both storage proteins are sequestered into the same area of protein.

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.

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).

Interactions of airborne methyl jasmonate with vegetative storage protein gene and protein accumulation and biomass partitioning in Populus plants

2000 ◽  
Vol 30 (7) ◽  
pp. 1106-1113 ◽  
Author(s):  
T Beardmore ◽  
S Wetzel ◽  
M Kalous
Keyword(s):  
Methyl Jasmonate ◽  
Storage Protein ◽  
Storage Proteins ◽  
Nitrogen Concentration ◽  
Protein Accumulation ◽  
Vegetative Storage Protein ◽  
Short Term ◽  
Specific Expression ◽  
Vegetative Storage Proteins

In young poplar (Populus nigra Muench × Populus maximowiczii A. Henry) plants, vegetative storage proteins (VSPs), the bark storage protein (BSP), and (or) wound-inducible 4 protein (WIN4) mRNAs were present in the apical and basal leaves and in the basal leaves, respectively. VSPs accumulated in the apical leaves and to a lesser extent in the stem. The response of the plants to 20 µM airborne methyl jasmonate (MJ) was examined in four parts ( apical and basal leaves, stem, and roots) in both short-term (within 72 h) and long-term (1, 2, 3, and 4 weeks) experiments. In the short-term, MJ-treated plants either induced or increased the part-specific expression of win4 and bsp, and accumulation of BSP and (or) WIN4. In the long-term, MJ treatment resulted in part-specific alterations in protein and nitrogen concentration and further altered BSP and WIN4 accumulation. The MJ-treated plants increased both the biomass allocation to the stem, without a change in the relative growth rate, and the tolerance low temperature (-2°C). Together, these results suggest the BSP and WIN4 are both involved in short-term N cycling and that exogenous MJ treatment promotes changes in nitrogen metabolism in poplar.

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