Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

• DOI: 10.1002/pro.4989
• Publication Date: 2024-04-25T05:29:13Z
• Authors: Itzell Hernández‐...; Tobias Rindfleisch; Jessica Alpers; Martin Dulle; Christopher J. Ga...; Patrick Knox‐Brown; Markus S. Miettinen; Gergely Nagy; Julio M. Pusterla; Agata Rekas; Keyun Shou; Andreas M. Stadler; Dirk Walther; Martin Wolff; Ellen Zuther; Anja Thalhammer
• Keywords: Structural plasticity; Intrinsically Disordered Proteins

Intrinsically disordered late embryogenesis abundant (LEA) proteins play a central role in the tolerance of plants and other organisms to dehydration brought upon, for example, by freezing temperatures, high salt concentration, drought or desiccation, many LEA have been found stabilize dehydration-sensitive cellular structures. Their conformational ensembles are highly sensitive environment, allowing them undergo changes adopt ordered secondary quaternary structures participate formation membraneless organelles. In an interdisciplinary approach, we discovered how functional diversity Arabidopsis thaliana protein COR15A vitro is encoded its structural repertoire, with stabilization membranes being achieved at level structure enzymes accomplished oligomeric complexes. We provide molecular details on intra- inter-monomeric helix-helix interactions, demonstrate oligomerization driven α-helical recognition feature (α-MoRF) rationale that noncanonical, loosely packed, right-handed coiled-coils might be recurring theme homo- hetero-oligomerization proteins.