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| Main Authors: | , , , , , , , , , , , , , , , |
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| Format: | Artículo Open Access |
| Published: |
Wiley
2024
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| Online Access: | https://onlinelibrary.wiley.com/doi/10.1002/pro.4989 |
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Table of Contents:
- Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity Itzell Hernández‐Sánchez Tobias Rindfleisch Jessica Alpers Martin Dulle Christopher J. Garvey 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 Protein Science AbstractIntrinsically 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, and many LEA proteins have been found to stabilize dehydration‐sensitive cellular structures. Their conformational ensembles are highly sensitive to the environment, allowing them to undergo conformational changes and adopt ordered secondary and quaternary structures and to participate in formation of membraneless organelles. In an interdisciplinary approach, we discovered how the functional diversity of the Arabidopsis thaliana LEA protein COR15A found in vitro is encoded in its structural repertoire, with the stabilization of membranes being achieved at the level of secondary structure and the stabilization of enzymes accomplished by the formation of oligomeric complexes. We provide molecular details on intra‐ and inter‐monomeric helix–helix interactions, demonstrate how oligomerization is driven by an α‐helical molecular recognition feature (α‐MoRF) and provide a rationale that the formation of noncanonical, loosely packed, right‐handed coiled‐coils might be a recurring theme for homo‐ and hetero‐oligomerization of LEA proteins. 10.1002/pro.4989 http://creativecommons.org/licenses/by/4.0/