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The effect of toxofilin on the structure and dynamics of monomeric actin.
Czimbalek, Lívia; Kollár, Veronika; Kardos, Roland; Lorinczy, Dénes; Nyitrai, Miklós; Hild, Gábor.
  • Czimbalek L; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary.
  • Kollár V; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary.
  • Kardos R; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary.
  • Lorinczy D; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary.
  • Nyitrai M; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary; Szentágothai Research Center, Pécs, Ifjúság Str. 34, H-7624, Hungary; MTA-PTE Nuclear-Mitochondrial Interactions Research Group, Pécs, Szigeti Str. 12, H-7624, Hungary.
  • Hild G; University of Pécs, Medical School, Department of Biophysics, Pécs, Szigeti Str. 12, H-7624, Hungary; Szentágothai Research Center, Pécs, Ifjúság Str. 34, H-7624, Hungary. Electronic address: gabor.hild@aok.pte.hu.
FEBS Lett ; 589(20 Pt B): 3085-9, 2015 Oct 07.
Article en En | MEDLINE | ID: mdl-26348398
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 21 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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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Termodinámica / Proteínas Protozoarias / Actinas / Proteínas de Capping de la Actina Límite: Animals Idioma: En Año: 2015 Tipo del documento: Article
Texto completo
Imprimir
XML
PubMed Links
Search on Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Termodinámica / Proteínas Protozoarias / Actinas / Proteínas de Capping de la Actina Límite: Animals Idioma: En Año: 2015 Tipo del documento: Article