22‐kD α‐zein‐mediated non‐zein protein accumulation in protein body of maize endosperm

2021 ◽  
Author(s):  
Yang Feng ◽  
Yafei Ma ◽  
Fan Feng ◽  
Xinze Chen ◽  
Weiwei Qi ◽  
...  
Keyword(s):  
Protein Body ◽  
Protein Accumulation ◽  
Maize Endosperm ◽  
Zein Protein

scholarly journals Zein Protein Interactions, Rather Than the Asymmetric Distribution of Zein mRNAs on Endoplasmic Reticulum Membranes, Influence Protein Body Formation in Maize Endosperm

2002 ◽  
Vol 14 (3) ◽  
pp. 655-672 ◽  
Author(s):  
Cheol Soo Kim ◽  
Young-min Woo ◽  
Amy M. Clore ◽  
Ronald J. Burnett ◽  
Newton P. Carneiro ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Interactions ◽  
Protein Body ◽  
Asymmetric Distribution ◽  
Maize Endosperm ◽  
Body Formation ◽  
Zein Protein

scholarly journals Nonredundant Function of Zeins and Their Correct Stoichiometric Ratio Drive Protein Body Formation in Maize Endosperm

2013 ◽  
Vol 162 (3) ◽  
pp. 1359-1369 ◽  
Author(s):  
X. Guo ◽  
L. Yuan ◽  
H. Chen ◽  
S. J. Sato ◽  
T. E. Clemente ◽  
...  
Keyword(s):  
Protein Body ◽  
Stoichiometric Ratio ◽  
Maize Endosperm ◽  
Body Formation

scholarly journals Opaque1 Encodes a Myosin XI Motor Protein That Is Required for Endoplasmic Reticulum Motility and Protein Body Formation in Maize Endosperm

2012 ◽  
Vol 24 (8) ◽  
pp. 3447-3462 ◽  
Author(s):  
Guifeng Wang ◽  
Fang Wang ◽  
Gang Wang ◽  
Fei Wang ◽  
Xiaowei Zhang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Body ◽  
Motor Protein ◽  
Maize Endosperm ◽  
Body Formation ◽  
Myosin Xi

Effect of thefloury-2 locus on protein body formation during maize endosperm development

PROTOPLASMA ◽  
1992 ◽  
Vol 171 (3-4) ◽  
pp. 123-133 ◽  
Author(s):  
C. R. Lending ◽  
B. A. Larkins
Keyword(s):  
Protein Body ◽  
Endosperm Development ◽  
Maize Endosperm ◽  
Body Formation

scholarly journals The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

2007 ◽  
Vol 19 (8) ◽  
pp. 2569-2582 ◽  
Author(s):  
David R. Holding ◽  
Marisa S. Otegui ◽  
Bailin Li ◽  
Robert B. Meeley ◽  
Thao Dam ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Body ◽  
Body Formation ◽  
Endoplasmic Reticulum Protein ◽  
Zein Protein

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.

Structural Aspects of Protein Accumulation in Developing Pea Cotyledons. I. Qualitative and Quantitative Changes in Parenchyma Cell Vacuoles

1979 ◽  
Vol 6 (1) ◽  
pp. 81 ◽  
Author(s):  
S Craig ◽  
DJ Goodchild ◽  
AR Hardham
Keyword(s):  
Cell Volume ◽  
Surface Area ◽  
Structural Changes ◽  
Light And Electron Microscopy ◽  
Parenchyma Cell ◽  
Protein Body ◽  
Average Diameter ◽  
Protein Bodies ◽  
Protein Accumulation ◽  
Parenchyma Cells

Structural changes in pea cotyledons during development were studied using light and electron microscopy. Changes in the vacuolar system and cytoplasm of cotyledon parenchyma cells, during the period of storage protein deposition, are reported. Eight days after flowering, the parenchyma cells each contain one or two large vacuoles that are replaced by progressively smaller vacuoles during the next 10 days of development. Stainable material that can be histochemically identified as protein appears on the inner surface of the vacuole tonoplast 8 days after flowering. These vacuoles become smaller and more frequent during development and the amount of proteinaceous material within each vacuole increases until, at days 16-20 after flowering, they become densely packed with protein and are described as protein bodies. At day 8, the vacuole(s) have an average diameter of 39 �m, an average volume of 41 000 �m� , representing 75 % of the cell volume, and a surface area of 5500 �m�. By day 20, the average protein body diameter has fallen to 1 �m. There are, however, approx. 175 000 such protein bodies per cell, occupying 91 500 �m� or approx. 20 % of the cell volume, and whose total surface area is 550 000 �m�. The surface to volume ratlo of the vacuole/protein bodies Increases 55 times between days 8 and 20. Apart from this increase in surface area available for possible entry of protein, no mechanism for such entry can be suggested from our nlicrographs.

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.

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