Metal ion – Dehydrin interactions investigated by affinity capillary electrophoresis and computer models

• Published in: Journal of plant physiology Vol. 216; pp. 219 - 228
• Main Authors: Nachbar, Markus, Mozafari, Mona, Krull, Friederike, Maul, Kai-Jorrit, Preu, Lutz, Hara, Masakazu, Wätzig, Hermann
• Format: Journal Article
• Language: English
• Published: Germany Elsevier GmbH 01.09.2017; Elsevier Science Ltd
• Subjects: Affinity; Affinity capillary electrophoresis; Arabidopsis - metabolism; Arabidopsis Proteins - metabolism; AtHIRD11; Binding; Capillary electrophoresis; Computer Simulation; Copper; Dehydrin; Electrophoresis; Electrophoresis, Capillary - methods; Environmental stress; Intrinsically disordered proteins; Ions; Mathematical models; Metal ions; Metals; Metals - metabolism; Models, Molecular; Molecular dynamics; Molecular model; Plant Proteins - metabolism; Proteins; Reactive oxygen species; Studies; CGE; Dehydrin; AtHIRD11; ACE; IDP; Intrinsically disordered proteins; MD; Molecular model; Affinity capillary electrophoresis; RMSD; HOS
• ISSN: 0176-1617; 1618-1328
• DOI: 10.1016/j.jplph.2017.06.006

Dehydrins are specialized proteins which are related to environmental stress tolerance in plants. The proteins can bind different metal ions and have versatile other functions such as reduction of reactive oxygen species and acting as transcription factor. The structure determination of proteins from this family is challenging, since they have a high number of disordered structure elements. Consequently, to determine the functionality of these proteins on a molecular basis a computed model is helpful. This work focuses on a model for the Arabidopsis thaliana dehydrin AtHIRD11. To develop a model which reflects experimental data from literature and own binding data from affinity capillary electrophoresis experiments, a more rigid state of this protein was chosen. The Cu2+-complex of this protein was formed and evaluated. The model explains some of the properties of the complexes. Possible Cu2+-bindings site were found and the change of conformations were investigated via molecular dynamics simulation. The AtHIRD11-Cu2+-complex is a first approach towards a complex model for a structural versatile protein, which is already sufficient to explain binding data and possible structure elements.