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Amyloid-like protein inclusions in tobacco transgenic plants.

ABSTRACT: The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered ?-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications.

SUBMITTER: Villar-Pique A

PROVIDER: S-EPMC2964307 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Amyloid-like protein inclusions in tobacco transgenic plants.

Villar-Piqué Anna A Sabaté Raimon R Lopera Oriol O Gibert Jordi J Torne Josep Maria JM Santos Mireya M Ventura Salvador S

PloS one 20101026 10

The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of ...[more]

PMID: 21049018

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