Functional homo- and heterodimeric actin capping proteins from the malaria parasite
| Autor: | Petri Kursula, Benjamin Götte, Moon Chatterjee, Ábris Ádám Bendes, Inari Kursula |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Protein Folding Plasmodium Actin Capping Proteins Actin-Capping Proteins Biophysics Protozoan Proteins Motility macromolecular substances Biochemistry Capping protein Protein filament 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Parasite hosting Animals Parasites Homodimer Molecular Biology Actin Heterodimer Core set Plasmodium (life cycle) biology Temperature Cell Biology biology.organism_classification Cell biology Malaria Solutions Actin Cytoskeleton 030104 developmental biology Monomer chemistry 030220 oncology & carcinogenesis Protein Multimerization Protein Binding |
| Zdroj: | Biochemical and biophysical research communications United States |
| Popis: | Actin capping proteins belong to the core set of proteins minimally required for actin-based motility and are present in virtually all eukaryotic cells. They bind to the fast-growing barbed end of an actin filament, preventing addition and loss of monomers, thus restricting growth to the slow-growing pointed end. Actin capping proteins are usually heterodimers of two subunits. The Plasmodium orthologs are an exception, as their α subunits are able to form homodimers. We show here that, while the β subunit alone is unstable, the α subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the αα homo- and αβ heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical αβ heterodimers, although certain rearrangements at the interface must be required. Both homo- and heterodimers bind to actin filaments in a roughly equimolar ratio, indicating they may also bind other sites than barbed ends. |
| Databáze: | OpenAIRE |
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