Protein reservoirs of seeds are composites of amyloid and amyloid-like structures

Abstract

AbstractThe functional roles of amyloids are known across diverse species, but their natural presence in plants remains underexplored. We show that monocot and dicot seed storage proteins, owing to their aggregated state, similar to protein-bodies of other species, are amyloidic. By using gold-standard amyloid probes, we reveal that the seed storage proteins exhibit a speckled pattern of amyloids interspersed in an amyloid-like matrix, suggesting their composite nature. Moreover, these structures degrade in a stepwise manner during germination and are sensitive to gibberellic acid.