Interaction of formin FH2 with skeletal muscle actin. EPR and DSC studies
| Autor: | Pál Gróf, Miklós Nyitrai, Tünde Kupi, József Belágyi |
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| Rok vydání: | 2013 |
| Předmět: |
Fetal Proteins
Conformational change Hot Temperature Maleimido-TEMPO Biophysics Formins macromolecular substances Formin 03 medical and health sciences Protein structure Animals Muscle Skeletal Protein Structure Quaternary Cytoskeleton Actin 030304 developmental biology Original Paper 0303 health sciences Calorimetry Differential Scanning biology Protein Stability Chemistry Microfilament Proteins fungi 030302 biochemistry & molecular biology Electron Spin Resonance Spectroscopy Nuclear Proteins Actin remodeling General Medicine Actin cytoskeleton Actins Protein Structure Tertiary Cell biology Protein conformation biology.protein MDia1 Protein Multimerization Electron paramagnetic resonance Protein Binding |
| Zdroj: | European Biophysics Journal |
| ISSN: | 1432-1017 0175-7571 |
| DOI: | 10.1007/s00249-013-0922-0 |
| Popis: | Formins are highly conserved proteins that are essential in the formation and regulation of the actin cytoskeleton. The formin homology 2 (FH2) domain is responsible for actin binding and acts as an important nucleating factor in eukaryotic cells. In this work EPR and DSC were used to investigate the properties of the mDia1-FH2 formin fragment and its interaction with actin. MDia1-FH2 was labeled with a maleimide spin probe (MSL). EPR results suggested that the MSL was attached to a single SH group in the FH2. In DSC and temperature-dependent EPR experiments we observed that mDia1-FH2 has a flexible structure and observed a major temperature-induced conformational change at 41 °C. The results also confirmed the previous observation obtained by fluorescence methods that formin binding can destabilize the structure of actin filaments. In the EPR experiments the intermolecular connection between the monomers of formin dimers proved to be flexible. Considering the complex molecular mechanisms underlying the cellular roles of formins this internal flexibility of the dimers is probably important for manifestation of their biological functions. Electronic supplementary material The online version of this article (doi:10.1007/s00249-013-0922-0) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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