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

Autor: Jan Petersen, Dorothea Bartels, Horst Röhrig, Steffen Pierog, Sylvia K. Eriksson, Thomas Colby, Pia Harryson
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Journal of Experimental Botany
ISSN: 1460-2431
0022-0957
Popis: 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 α-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. Abbreviations: ABA abscisic acid; CD circular dichroism; CS citrate synthase; IDP intrinsically disordered protein; LDH lactate dehydrogenase; LEA late embryogenesis abundant; PA phosphatidic acid; PC phosphatidylcholine; TFE trifluoroethanol.
Databáze: OpenAIRE