scholarly journals Protein body formation in the endoplasmic reticulum as an evolution of storage protein sorting to vacuoles: insights from maize γ-zein

2014 ◽  
Vol 5 ◽  
Author(s):  
Davide Mainieri ◽  
Francesca Morandini ◽  
Marie Maîtrejean ◽  
Andrea Saccani ◽  
Emanuela Pedrazzini ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Storage Protein ◽  
Protein Sorting ◽  
Protein Body ◽  
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

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

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 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

Endosperm Morphology and Protein Body Formation in Developing Wheat Grain

1981 ◽  
Vol 8 (1) ◽  
pp. 5 ◽  
Author(s):  
WP Campbell ◽  
JW Lee ◽  
TP O'brien ◽  
MG Smart
Keyword(s):  
Endoplasmic Reticulum ◽  
Culture Medium ◽  
Sucrose Concentration ◽  
Light And Electron Microscopy ◽  
Starch Synthesis ◽  
Protein Body ◽  
Protein Bodies ◽  
Wheat Grain ◽  
Body Formation ◽  
Intact Plants

The development of wheat grain from intact plants and from detached ears growing in culture has been studied by light and electron microscopy. Provided the sucrose concentration was at a level sufficient to maintain a normal rate of starch synthesis, the endosperm morphology of grain from cultured ears was essentially identical to that of endosperm from intact plants. If, however, sucrose concentration in the culture medium was very low (0.25%), some morphological abnormalities occurred in the endosperm near the crease and adjacent to the seed coat. The synthesis of storage protein in the endosperm is believed to occur largely on polyribosomes attached to endoplasmic reticulum even at the earliest stages of development. Protein bodies are always surrounded by a single membrane, the origin of which may vary. Some protein bodies arise by distention of the endoplasmic reticulum and clearly the membrane here represents the sac into which the protein is discharged after synthesis. In other cases the bounding membrane may be that of a true vacuole or it may be dictyosomal in origin. The methods by which it is suggested that protein bodies are formed in wheat endosperm have parallels in other seeds, although there are some significant differences.

Sign in / Sign up

Export Citation Format

Share Document