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Amyloid-like protein inclusions in tobacco transgenic plants.

Villar-Piqué A, Sabaté R, Lopera O, Gibert J, Torne JM, Santos M, Ventura S - PLoS ONE (2010)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.

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 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.

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Related in: MedlinePlus

Maize TGZ forms protein inclusions in transplastomic tobacco chloroplasts.A) Aspect of wild type tobacco plant. B) Aspect of tgz-transplastomic tobacco plant. C) TEM image of a tgz-transplastomic tobacco chloroplast. A high number of appressed thylakoid membranes (arrows), membrane interruptions and IB presence are shown. Inside: subcellular immunolocalization of TGZ protein in the IB of a tobacco tgz-transformed chloroplast using an anti-TGZ antibody (1:3000) (see M & M). D) TEM image of a WT tobacco chloroplast showing normal thylakoid membranes and interconnexions. IB, inclusion body; T, thylacoids.
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pone-0013625-g003: Maize TGZ forms protein inclusions in transplastomic tobacco chloroplasts.A) Aspect of wild type tobacco plant. B) Aspect of tgz-transplastomic tobacco plant. C) TEM image of a tgz-transplastomic tobacco chloroplast. A high number of appressed thylakoid membranes (arrows), membrane interruptions and IB presence are shown. Inside: subcellular immunolocalization of TGZ protein in the IB of a tobacco tgz-transformed chloroplast using an anti-TGZ antibody (1:3000) (see M & M). D) TEM image of a WT tobacco chloroplast showing normal thylakoid membranes and interconnexions. IB, inclusion body; T, thylacoids.

Mentions: Homoplasmic tobacco tgz-transgenic plants presented abnormal phenotype with respect to the leaf colour, having pigment deficiencies (Fig. 3A) and thylakoid appression abnormalities (Figure 3B). The TGZ protein was immunolocalized into chloroplast inclusion bodies (Figure 3C insert), suggesting that in the plant the protein is present in an at least partially aggregated state, which might coexist with functional conformations as shown for bacterial inclusion bodies [24]. The thylakoids in the chloroplasts of non-transgenic plants displayed a normal arrangement with grana stacks consisting of 15–20 tightly appressed thylakoid membranes interconnected by stroma thylakoids (Figure 3D).


Amyloid-like protein inclusions in tobacco transgenic plants.

Villar-Piqué A, Sabaté R, Lopera O, Gibert J, Torne JM, Santos M, Ventura S - PLoS ONE (2010)

Maize TGZ forms protein inclusions in transplastomic tobacco chloroplasts.A) Aspect of wild type tobacco plant. B) Aspect of tgz-transplastomic tobacco plant. C) TEM image of a tgz-transplastomic tobacco chloroplast. A high number of appressed thylakoid membranes (arrows), membrane interruptions and IB presence are shown. Inside: subcellular immunolocalization of TGZ protein in the IB of a tobacco tgz-transformed chloroplast using an anti-TGZ antibody (1:3000) (see M & M). D) TEM image of a WT tobacco chloroplast showing normal thylakoid membranes and interconnexions. IB, inclusion body; T, thylacoids.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2964307&req=5

pone-0013625-g003: Maize TGZ forms protein inclusions in transplastomic tobacco chloroplasts.A) Aspect of wild type tobacco plant. B) Aspect of tgz-transplastomic tobacco plant. C) TEM image of a tgz-transplastomic tobacco chloroplast. A high number of appressed thylakoid membranes (arrows), membrane interruptions and IB presence are shown. Inside: subcellular immunolocalization of TGZ protein in the IB of a tobacco tgz-transformed chloroplast using an anti-TGZ antibody (1:3000) (see M & M). D) TEM image of a WT tobacco chloroplast showing normal thylakoid membranes and interconnexions. IB, inclusion body; T, thylacoids.
Mentions: Homoplasmic tobacco tgz-transgenic plants presented abnormal phenotype with respect to the leaf colour, having pigment deficiencies (Fig. 3A) and thylakoid appression abnormalities (Figure 3B). The TGZ protein was immunolocalized into chloroplast inclusion bodies (Figure 3C insert), suggesting that in the plant the protein is present in an at least partially aggregated state, which might coexist with functional conformations as shown for bacterial inclusion bodies [24]. The thylakoids in the chloroplasts of non-transgenic plants displayed a normal arrangement with grana stacks consisting of 15–20 tightly appressed thylakoid membranes interconnected by stroma thylakoids (Figure 3D).

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.

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 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.

Show MeSH
Related in: MedlinePlus