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The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions

Andersson, Jenny Marie LU ; Pham, Quoc Dat LU ; Mateos, Helena ; Eriksson, Sylvia ; Harryson, Pia and Sparr, Emma LU (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
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organization
publishing date
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
  • pmid:32404333
  • scopus:85087532371
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
2020-07-22 04:21:49
@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},
  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},
}