Preferential adsorption to air-water interfaces: a novel cryoprotective mechanism for LEA proteins.
Adsorption
Air
Animals
Arabidopsis Proteins
/ chemistry
Biophysical Phenomena
Citrate (si)-Synthase
/ chemistry
Cryoprotective Agents
/ chemistry
Freezing
Helminth Proteins
/ chemistry
Intrinsically Disordered Proteins
/ chemistry
Neutron Diffraction
Protein Aggregates
Protein Folding
Protein Stability
Recombinant Proteins
/ chemistry
Rhabditida
/ chemistry
Scattering, Small Angle
Stress, Physiological
Swine
Water
anhydrobiosis
freeze–thaw
neutron reflection
protein aggregation
stress tolerance
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
10 04 2019
10 04 2019
Historique:
received:
23
11
2018
revised:
18
03
2019
accepted:
20
03
2019
pubmed:
23
3
2019
medline:
11
2
2020
entrez:
23
3
2019
Statut:
epublish
Résumé
Late embryogenesis abundant (LEA) proteins comprise a diverse family whose members play a key role in abiotic stress tolerance. As intrinsically disordered proteins, LEA proteins are highly hydrophilic and inherently stress tolerant. They have been shown to stabilise multiple client proteins under a variety of stresses, but current hypotheses do not fully explain how such broad range stabilisation is achieved. Here, using neutron reflection and surface tension experiments, we examine in detail the mechanism by which model LEA proteins, AavLEA1 and ERD10, protect the enzyme citrate synthase (CS) from aggregation during freeze-thaw. We find that a major contributing factor to CS aggregation is the formation of air bubbles during the freeze-thaw process. This greatly increases the air-water interfacial area, which is known to be detrimental to folded protein stability. Both model LEA proteins preferentially adsorb to this interface and compete with CS, thereby reducing surface-induced aggregation. This novel surface activity provides a general mechanism by which diverse members of the LEA protein family might function to provide aggregation protection that is not specific to the client protein.
Identifiants
pubmed: 30898848
pii: BCJ20180901
doi: 10.1042/BCJ20180901
pmc: PMC6458962
doi:
Substances chimiques
Arabidopsis Proteins
0
Cryoprotective Agents
0
ERD10 protein, Arabidopsis
0
Helminth Proteins
0
Intrinsically Disordered Proteins
0
Protein Aggregates
0
Recombinant Proteins
0
Water
059QF0KO0R
Citrate (si)-Synthase
EC 2.3.3.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1121-1135Informations de copyright
© 2019 The Author(s).
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