One Vacuole or two Vacuoles: Do Protein Storage Vacuoles Arise de novo during Pea Cotyledon Development?

1995 ◽  
Vol 145 (5-6) ◽  
pp. 654-664 ◽  
Author(s):  
David G. Robinson ◽  
Birgit Hoh ◽  
Giselbert Hinz ◽  
Byung-Kap Jeong
Keyword(s):  
De Novo ◽  
Protein Storage ◽  
Protein Storage Vacuoles

scholarly journals Protein storage vacuoles form de novo during pea cotyledon development

1995 ◽  
Vol 108 (1) ◽  
pp. 299-310 ◽  
Author(s):  
B. Hoh ◽  
G. Hinz ◽  
B.K. Jeong ◽  
D.G. Robinson
Keyword(s):  
Membrane Protein ◽  
De Novo ◽  
Storage Proteins ◽  
Protein Body ◽  
Membrane System ◽  
Intermediate Stage ◽  
Integral Membrane Protein ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole

We have investigated the formation of protein storage vacuoles in peas (Pisum sativum L.) in order to determine whether this organelle arises de novo during cotyledon development. A comparison of different stages in cotyledon development indicates that soluble protease activities decline and the amounts of storage proteins and the integral membrane protein of the protein body, alpha-TIP, increase during seed maturation. On linear sucrose density gradients we have been able to distinguish between two separate vesicle populations: one enriched in alpha-TIP, and one in TIP-Ma 27, a membrane protein characteristic of vegetative vacuoles. Both vesicle populations possess, however, PPase and V-ATPase activities. Conventionally fixed cotyledonary tissue at an intermediate stage in cotyledon development reveals the presence of a complex tubular-cisternal membrane system that seems to surround the pre-existing vacuoles. The latter gradually become compressed as a result of dilation of the former membrane system. This was confirmed immunocytochemically with the TIP-Ma 27 antiserum. Deposits of the storage proteins vicilin and legumin in the lumen, and the presence of alpha-TIP in the membranes of the expanding membrane system provide evidence of its identity as a precursor to the protein storage vacuole.

scholarly journals A Novel Membrane Protein That Is Transported to Protein Storage Vacuoles via Precursor-Accumulating Vesicles

2001 ◽  
Vol 13 (10) ◽  
pp. 2361-2372 ◽  
Author(s):  
Naoto Mitsuhashi ◽  
Yasuko Hayashi ◽  
Yasuko Koumoto ◽  
Tomoo Shimada ◽  
Tomoko Fukasawa-Akada ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Storage ◽  
Protein Storage Vacuoles

Targeting and processing of membrane-anchored YFP fusion proteins to protein storage vacuoles in transgenic tobacco seeds

2005 ◽  
Vol 15 (4) ◽  
pp. 361-364 ◽  
Author(s):  
Ka Leung Fung ◽  
Yin Fun Yim ◽  
Yu Chung Tse ◽  
Yansong Miao ◽  
Samuel S.M. Sun ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Fusion Proteins ◽  
Seed Protein ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Pharmaceutical Proteins ◽  
Tobacco Seeds ◽  
Foreign Proteins

Seeds that store proteins in protein storage vacuoles are attractive bioreactors for producing and storing large amounts of pharmaceutical proteins. However, foreign proteins expressed in transgenic plants are subjected to the delivery and modification processes present within plant cells. Here, it is demonstrated that unique membrane sequences deliver a yellow fluorescent protein (YFP) to the seed protein storage vacuoles in transgenic tobacco (Nicotiana tabacum L.) plants, where the YFP is then separated from its membrane anchors. This precise targeting and separation is required for the successful delivery of useful proteins to seed protein storage vacuoles for their stable accumulation in transgenic crops.

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.

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