The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions
(2020) In Journal of Lipid Research 61(7). p.1014-1024- Abstract
A major challenge to plant growth and survival are changes in temperature and diminishing water supply. During acute temperature and water stress, plants often express stress proteins, such as dehydrins, which are intrinsically disordered hydrophilic proteins. In this article, we investigated how the dehydrin Lti30 from Arabidopsis thaliana stabilizes membrane systems that are exposed to large changes in hydration. We also compared the effects of Lti30 on membranes with those of the simple osmolytes urea and trimethylamine N-oxide. Using X-ray diffraction and solid-state NMR, we studied lipid-protein self-assembly at varying hydration levels. We made the following observations: 1) the association of Lti30 with anionic membranes relies... (More)
A major challenge to plant growth and survival are changes in temperature and diminishing water supply. During acute temperature and water stress, plants often express stress proteins, such as dehydrins, which are intrinsically disordered hydrophilic proteins. In this article, we investigated how the dehydrin Lti30 from Arabidopsis thaliana stabilizes membrane systems that are exposed to large changes in hydration. We also compared the effects of Lti30 on membranes with those of the simple osmolytes urea and trimethylamine N-oxide. Using X-ray diffraction and solid-state NMR, we studied lipid-protein self-assembly at varying hydration levels. We made the following observations: 1) the association of Lti30 with anionic membranes relies on electrostatic attraction, and the protein is located in the bilayer interfacial membrane region; 2) Lti30 can stabilize the lamellar multilayer structure, making it insensitive to variations in water content; 3) in lipid systems with a composition similar to those present in some seeds and plants, dehydrin can prevent the formation of nonlamellar phases upon drying, which may be crucial for maintaining membrane integrity; and 4) Lti30 stabilizes bilayer structures both at high and low water contents, whereas the small osmolyte molecules mainly prevent dehydration-induced transitions. These results corroborate the idea that dehydrins are part of a sensitive and multifaceted regulatory mechanism that protects plant cells against stress.
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- author
- Andersson, Jenny Marie LU ; Pham, Quoc Dat LU ; Mateos, Helena ; Eriksson, Sylvia ; Harryson, Pia and Sparr, Emma LU
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- desiccation, osmolytes, protein, self-assembly, trimethylamine N-oxide, urea
- in
- Journal of Lipid Research
- volume
- 61
- issue
- 7
- pages
- 11 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:85087532371
- pmid:32404333
- ISSN
- 1539-7262
- DOI
- 10.1194/jlr.RA120000624
- language
- English
- LU publication?
- yes
- id
- 52b0701f-4281-4d90-8ed4-3b1d93193436
- date added to LUP
- 2020-07-15 12:42:18
- date last changed
- 2024-04-17 12:33:41
@article{52b0701f-4281-4d90-8ed4-3b1d93193436,
abstract = {{<p>A major challenge to plant growth and survival are changes in temperature and diminishing water supply. During acute temperature and water stress, plants often express stress proteins, such as dehydrins, which are intrinsically disordered hydrophilic proteins. In this article, we investigated how the dehydrin Lti30 from Arabidopsis thaliana stabilizes membrane systems that are exposed to large changes in hydration. We also compared the effects of Lti30 on membranes with those of the simple osmolytes urea and trimethylamine N-oxide. Using X-ray diffraction and solid-state NMR, we studied lipid-protein self-assembly at varying hydration levels. We made the following observations: 1) the association of Lti30 with anionic membranes relies on electrostatic attraction, and the protein is located in the bilayer interfacial membrane region; 2) Lti30 can stabilize the lamellar multilayer structure, making it insensitive to variations in water content; 3) in lipid systems with a composition similar to those present in some seeds and plants, dehydrin can prevent the formation of nonlamellar phases upon drying, which may be crucial for maintaining membrane integrity; and 4) Lti30 stabilizes bilayer structures both at high and low water contents, whereas the small osmolyte molecules mainly prevent dehydration-induced transitions. These results corroborate the idea that dehydrins are part of a sensitive and multifaceted regulatory mechanism that protects plant cells against stress.</p>}},
author = {{Andersson, Jenny Marie and Pham, Quoc Dat and Mateos, Helena and Eriksson, Sylvia and Harryson, Pia and Sparr, Emma}},
issn = {{1539-7262}},
keywords = {{desiccation; osmolytes; protein; self-assembly; trimethylamine N-oxide; urea}},
language = {{eng}},
number = {{7}},
pages = {{1014--1024}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Lipid Research}},
title = {{The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions}},
url = {{http://dx.doi.org/10.1194/jlr.RA120000624}},
doi = {{10.1194/jlr.RA120000624}},
volume = {{61}},
year = {{2020}},
}