Amyloids and prions in plants: Facts and perspectives

Figures & data

TABLE 1. Amyloidogenic proteins in plants.

			Amyloid properties were shown:^*
Protein	Function	Species	in vivo	in vitro	Reference
Proteins of algae extracellular polymeric substances (EPS)^**	Attachment to surface	Coccomyxa sp., Glaphyrella trebouxiodes и Prasiola linearis (algae)	+	−	46, 47
Luminidependens (LD)	Autonomous Flowering Pathway (AFP) component	Arabidopsis thaliana (rockcress), Saccharomyces cerevisiae (yeast)^***	±	−	53
Flowering Locus PA (FPA)	AFP component	Arabidopsis thaliana (rockcress), Saccharomyces cerevisiae (yeast)^***	±	−	53
Flowering Locus CA (FCA)	AFP component	Arabidopsis thaliana (rockcress), Saccharomyces cerevisiae (yeast)^***	±	−	53
Pro-hevein С-terminal domain	Latex component, protective function	Hevea brasiliensis (rubber tree)	−	+	66
Monellin	Unknown, has a sweet taste for human	Dioscoreophyllum cumminsii	−	±	64
Maize transglutaminase (TGZ)	Posttranslational modification of proteins	Zea mays (corn), Nicotiana tabacum (tobacco)^****	±	+	65
RsAFP-19 peptide	RsAFP1 and RsAFP2 defensins fragment, fungicide	Raphanus sativus (radish)	−	+	69
Cn-AMP2 peptide	Antimicrobial peptide of liquid endosperm	Cocos nucifera (coconut tree)	−	+	68
Peptides resulting after the limited proteolysis of the seed storage proteins^**	Nutrient storage	Glycine max (soybean), Pisum sativum (pea), Triticum aestivum (wheat)	±	−	91–93

* «+» Amyloid properties were completely validated; «±» at least one of the amyloid properties was shown (formation of detergent-resistant aggregates in vivo, fibril formation in vitro, apple-green birefringence upon Congo red binding, or increase in Thioflavin-T fluorescence); «-» amyloid properties were not shown.

** Particular proteins were not identified.

*** Amyloid properties of these A. thaliana proteins were investigated in the heterologous S. cerevisiae system.

**** Amyloid properties of Z. mays TGZ protein were shown under overexpression in transplastomic N. tabacum plants.

FIGURE 1. Location of potentially amyloidogenic proteins in plants. A schematic illustration of the plant is shown. The names of proteins or peptides, whose amyloid properties were partially characterized in vivo (green) and in vitro (orange), and proteins, whose fragments have amyloidogenic properties (black), are indicated. The data on these proteins and peptides are summarized in Table 1.