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The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2012 (English)In: Journal of Experimental Botany, ISSN 0022-0957, E-ISSN 1460-2431, Vol. 63, no 13, 4919-4929 p.Article in journal (Refereed) Published
Abstract [en]

The late embryogenesis abundant (LEA)-like protein CDeT11-24 is one of the major desiccation-related phosphoproteins of the resurrection plant Craterostigma plantagineum. In this study, it was shown that CDeT11-24 is mostly intrinsically disordered and protects two different enzymes, citrate synthase and lactate dehydrogenase, against damaging effects caused by desiccation. Lipid-binding assays revealed that CDeT11-24 is able to interact with phosphatidic acid, although electrostatic repulsion was expected due to the overall negative net charge of the protein under the tested physiological conditions. CDeT11-24 carries an N-terminal lysine-rich sequence, which is predicted to form an amphipathic alpha-helix. Analysis of the truncated CDeT11-24 protein identified this region to be responsible for both activities: enzyme protection and phosphatidic acid interaction. Possible functions of the CDeT11-24 protein are discussed in the context of desiccation tolerance.

Place, publisher, year, edition, pages
2012. Vol. 63, no 13, 4919-4929 p.
Keyword [en]
desiccation tolerance, lipid binding, K-segment, molecular shield
National Category
Biological Sciences
Research subject
URN: urn:nbn:se:su:diva-81544DOI: 10.1093/jxb/ers173ISI: 000308010700019OAI: diva2:564105


Available from: 2012-11-01 Created: 2012-10-25 Last updated: 2015-08-21Bibliographically approved

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Eriksson, Sylvia K.Harryson, Pia
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