Amyloid-like protein inclusions in tobacco transgenic plants.
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 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.
Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Anna
A
Villar-Piqué
Raimon
R
Sabaté
Oriol
O
Lopera
Jordi
J
Gibert
Josep Maria
JM
Torne
Mireya
M
Santos
Salvador
S
Ventura
D000682:Amyloid / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D046529:Microscopy, Electron, Transmission; D030821:Plants, Genetically Modified / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D014026:Nicotiana / Q000378:metabolism*; D011503:Transglutaminases / Q000378:metabolism; D003313:Zea mays / Q000201:enzymology
D000682:Amyloid; D011503:Transglutaminases