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

Andersson, Jenny MarieLund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH (författare)

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 fromArabidopsis thalianastabilizes 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 trimethylamineN-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; and4) 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.

NATURVETENSKAP Biologi hsv//swe
NATURAL SCIENCES Biological Sciences hsv//eng
NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
protein
self-assembly
osmolytes
urea
trimethylamineN-oxide
desiccation
desiccation
osmolytes
protein
self-assembly
trimethylamine N-oxide
urea

Pham, Quoc DatLund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkem-dph (författare)
Mateos, HelenaLund University (författare)
Eriksson, SylviaStockholm University,Stockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)syer3190 (författare)
Harryson, PiaStockholm University,Stockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)hpia (författare)
Sparr, EmmaLund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fk1-esp (författare)
Fysikalisk kemiEnheten för fysikalisk och teoretisk kemi (creator_code:org_t)

Av författaren/redakt...: Andersson, Jenny ...; Pham, Quoc Dat; Mateos, Helena; Eriksson, Sylvia; Harryson, Pia; Sparr, Emma

Om ämnet

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.