Amyloid-like protein inclusions in tobacco transgenic plants

Anna Villar-Piqué, Raimon Sabaté, Oriol Lopera, Jordi Gibert, Josep Maria Torne, Mireya Santos, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

34 Citations (Scopus)

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 b-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. © 2010 Villar-Piqué et al.
Original languageEnglish
Article numbere13625
JournalPLoS ONE
Volume5
DOIs
Publication statusPublished - 17 Nov 2010

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