The effect of mouse twinfilin-1 on the structure and dynamics of monomeric actin.

Autor:	Takács-Kollár V; 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; University of Pécs, Medical School, Department of Radiology, Pécs, Ifjúság Str. 13. H-7624, Hungary. Electronic address: gabor.hild@aok.pte.hu.
Jazyk:	angličtina
Zdroj:	Biochimica et biophysica acta [Biochim Biophys Acta] 2016 Jul; Vol. 1864 (7), pp. 840-6. Date of Electronic Publication: 2016 Apr 12.
DOI:	10.1016/j.bbapap.2016.04.002
Abstrakt:	The effect of twinfilin-1 on the structure and dynamics of monomeric actin was investigated with fluorescence spectroscopy and differential scanning calorimetry experiments. Fluorescence anisotropy measurements proved that G-actin and twinfilin-1 could form a complex. Due to the formation of the complexes the dissociation of the nucleotide slowed down from the nucleotide-binding pocket of actin. Fluorescence quenching experiments showed that the accessibility of the actin bound ε-ATP decreased in the presence of twinfilin-1. Temperature dependent fluorescence resonance energy transfer and differential scanning calorimetry experiments revealed that the protein matrix of actin becomes more rigid and more heat resistant in the presence of twinfilin-1. The results suggest that the nucleotide binding cleft shifted into a more closed and stable conformational state of actin in the presence of twinfilin-1. (Copyright © 2016 Elsevier B.V. All rights reserved.)
Databáze:	MEDLINE
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