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Tunable membrane binding of the intrinsically disordered dehydrin Lti30, a cold-induced plant stress protein
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91 Stockholm, Sweden.
Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2011 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 23, no 6, 2391-2404 p.Article in journal (Refereed) Published
Abstract [en]

Dehydrins are intrinsically disordered plant proteins whose expression is upregulated under conditions of desiccation and cold stress. Their molecular function in ensuring plant survival is not yet known, but several studies suggest their involvement in membrane stabilization. The dehydrins are characterized by a broad repertoire of conserved and repetitive sequences, out of which the archetypical K-segment has been implicated in membrane binding. To elucidate the molecular mechanism of these K-segments, we examined the interaction between lipid membranes and a dehydrin with a basic functional sequence composition: Lti30, comprising only K-segments. Our results show that Lti30 interacts electrostatically with vesicles of both zwitterionic (phosphatidyl choline) and negatively charged phospholipids (phosphatidyl glycerol, phosphatidyl serine, and phosphatidic acid) with a stronger binding to membranes with high negative surface potential. The membrane interaction lowers the temperature of the main lipid phase transition, consistent with Lti30's proposed role in cold tolerance. Moreover, the membrane binding promotes the assembly of lipid vesicles into large and easily distinguishable aggregates. Using these aggregates as binding markers, we identify three factors that regulate the lipid interaction of Lti30 in vitro: (1) a pH dependent His on/off switch, (2) phosphorylation by protein kinase C, and (3) reversal of membrane binding by proteolytic digest.

Place, publisher, year, edition, pages
2011. Vol. 23, no 6, 2391-2404 p.
National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-44954DOI: 10.1105/tpc.111.085183PubMedID: 21665998OAI: diva2:423377
Available from: 2011-06-15 Created: 2011-06-15 Last updated: 2011-09-28Bibliographically approved

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Kutzer, MichaelProcek, JanGröbner, Gerhard
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Umeå Plant Science Centre (UPSC)Department of Chemistry
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