Multiple internal sorting determinants can contribute to the trafficking of cruciferin to protein storage vacuoles

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.

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Preparative Procedures Markedly Influence the Appearance and Structural Integrity of Protein Storage Vacuoles in Soybean Seeds

Journal of Agricultural and Food Chemistry ◽

10.1021/jf0735228 ◽

2008 ◽

Vol 56 (9) ◽

pp. 2907-2912 ◽

Cited By ~ 7

Author(s):

Hari B. Krishnan

Keyword(s):

Structural Integrity ◽

Soybean Seeds ◽

Protein Storage ◽

Protein Storage Vacuoles

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Immunolocalization of ricin accumulation during castor bean (Ricinus communis L.) seed development

International Journal of Plant Biology ◽

10.4081/pb.2010.e12 ◽

2010 ◽

Vol 1 (2) ◽

pp. 12 ◽

Cited By ~ 9

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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