Abstract
Seed storage proteins, well-known for their nutritional functions are sequestered in protein bodies. However, their biophysical properties at the molecular level remain elusive. Based on the structure and function of protein bodies found in other organisms, we hypothesize that the seed protein bodies might be present as amyloid structures. When visualized with a molecular rotor Thioflavin-T and a recently discovered Proteostat® probe with enhanced sensitivity, the seed sections showed amyloid-like signatures in the protein storage bodies of the aleurone cells of monocots and cotyledon cells of dicots. To make the study compliant for amyloid detection, gold-standard Congo red dye was used. Positive apple-green birefringence due to Congo red affinity in some of the areas of ThT and Proteostat® binding, suggests the presence of both amyloid-like and amyloid deposits in the protein storage bodies. Further, diminishing amyloid signature in germinating seeds implies the degradation of these amyloid structures and their utilization. This study will open new research avenues for a detailed molecular-level understanding of the formation and utilization of aggregated protein bodies as well as their evolutionary roles.
Competing Interest Statement
The authors have declared no competing interest.
Footnotes
↵a The author(s) responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (https://academic.oup.com/plcell/pages/General-Instructions) is: Prof. A.K.Thakur (akthakur{at}iitk.ac.in).