Functional in vitro diversity of an intrinsically disordered plant protein during freeze-thawing is encoded by its structural plasticity.
freezing tolerance
functional plasticity
intrinsically disordered protein
late embryogenesis abundant protein
self‐assembly
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
May 2024
May 2024
Historique:
revised:
09
03
2024
received:
25
10
2023
accepted:
31
03
2024
medline:
25
4
2024
pubmed:
25
4
2024
entrez:
25
4
2024
Statut:
ppublish
Résumé
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, 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.
Substances chimiques
Arabidopsis Proteins
0
Intrinsically Disordered Proteins
0
COR15 protein, Arabidopsis
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e4989Subventions
Organisme : Trond Mohn Foundation
ID : BFS2017TMT01
Organisme : National Collaborative Research Infrastructure Strategy
ID : NDF8141
Organisme : National Collaborative Research Infrastructure Strategy
ID : NDF6449
Organisme : Spallation Neutron Source
ID : 30279.1
Informations de copyright
© 2024 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
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