Abstract Detail

Development and Structure

Sinha, Nabodita [1], Zahra, Talat [1], Thakur, Ashwani [1].

Protein reservoirs of seeds are composites of amyloid and amyloid-like structures facilitating germination.

The functional roles of amyloids are known across diverse species, but their natural presence in plants remains underexplored. Based on the structure and function of protein bodies found in other organisms, we hypothesize that the seed storage protein bodies (SSPB) may have amyloid structures for controlling physiological functions. Here we show that monocot and dicot SSPB exhibit a speckled-pattern of amyloids interspersed in an amyloid-like matrix, suggesting their composite nature. This is confirmed by amyloid-specific probes, amyloidogenic region scans, infrared signatures, reconstitution studies, and differential degradation during germination. The role of amyloidic composites in seed germination is proved by amyloid content, degradation inhibition and relevant germination parameters, using in-vitro SSPB, ex-vivo protoplasts and in-situ seed sections. The results open new research questions in understanding molecular details of SSPB assembly-disassembly and utilization, in addition to evolutionary roles of amyloid structure and function.

1 - Indian Institute of Technology Kanpur, Biological Science and Bioengineering, Lab 6, Kanpur, Uttar Pradesh, 208016, India

native seed
protein aggregate
functional traits.

Presentation Type: Oral Paper
Number: DS2006
Abstract ID:119
Candidate for Awards:Katherine Esau Award,Maynard F. Moseley Award

Copyright © 2000-2022, Botanical Society of America. All rights reserved