| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10869870 | FEBS Letters | 2015 | 5 Pages |
Abstract
The effects of toxofilin (an actin binding protein of Toxoplasma gondii) on G-actin was studied with spectroscopy techniques. Fluorescence anisotropy measurements proved that G-actin and toxofilin interact with 2:1 stoichiometry. The affinity of toxofilin to actin was also determined with a fluorescence anisotropy assay. Fluorescence quenching experiments showed that the accessibility of the actin bound ε-ATP decreased in the presence of toxofilin. The results can be explained by the shift of the nucleotide binding cleft into a closed conformational state. Differential scanning calorimetry measurements revealed that actin monomers become thermodynamically more stable due to the binding of toxofilin.
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Authors
LÃvia Czimbalek, Veronika Kollár, Roland Kardos, Dénes LÅrinczy, Miklós Nyitrai, Gábor Hild,