Amyloid fibril; Double PHD finger 3 (DPF3); Intrinsically disordered protein; Protein aggregation; Spectroscopy; Amyloid; Intrinsically Disordered Proteins; Protein Isoforms; Transcription Factors; Amyloid/chemistry; Protein Isoforms/metabolism; Transcription Factors/metabolism; Zinc Fingers; Intrinsically Disordered Proteins/chemistry; Structural Biology; Biochemistry; Molecular Biology; General Medicine
Abstract :
[en] Double PHD fingers 3 (DPF3) is a zinc finger protein, found in the BAF chromatin remodelling complex, and is involved in the regulation of gene expression. Two DPF3 isoforms have been identified, respectively named DPF3b and DPF3a. Very limited structural information is available for these isoforms, and their specific functionality still remains poorly studied. In a previous work, we have demonstrated the first evidence of DPF3a being a disordered protein sensitive to amyloid fibrillation. Intrinsically disordered proteins (IDPs) lack a defined tertiary structure, existing as a dynamic conformational ensemble, allowing them to act as hubs in protein-protein interaction networks. In the present study, we have more thoroughly characterised DPF3a in vitro behaviour, as well as unravelled and compared the structural properties of the DPF3b isoform, using an array of predictors and biophysical techniques. Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters. DPF3a appears to be more disordered than DPF3b, and exhibits more expanded conformations. Furthermore, we have shown that they both time-dependently aggregate into amyloid fibrils, as revealed by typical circular dichroism, deep-blue autofluorescence, and amyloid-dye binding assay fingerprints. Although spectroscopic and microscopic analyses have unveiled that they share a similar aggregation pathway, DPF3a fibrillates at a faster rate, likely through reordering of its C-terminal domain.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Mignon, Julien; Laboratoire de Chimie Physique des Biomolécules, UCPTS, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium. Electronic address: julien.mignon@unamur.be
Mottet, Denis ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques
Leyder, Tanguy; Laboratoire de Chimie Physique des Biomolécules, UCPTS, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium. Electronic address: tanguy.leyder@student.unamur.be
Uversky, Vladimir N; Department of Molecular Medicine, USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address: vuversky@usf.edu
Perpète, Eric A; Laboratoire de Chimie Physique des Biomolécules, UCPTS, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium, Institute of Life, Earth and Environment (ILEE), University of Namur, Namur, Belgium. Electronic address: eric.perpete@unamur.be
Michaux, Catherine; Laboratoire de Chimie Physique des Biomolécules, UCPTS, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium, Namur Institute of Structured Matter (NISM), University of Namur, Namur, Belgium, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium. Electronic address: catherine.michaux@unamur.be
Language :
English
Title :
Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a.
Publication date :
01 October 2022
Journal title :
International Journal of Biological Macromolecules
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
Funding text :
Authors are appreciative to the Research Unit in Biology of Microorganisms, as well as to the MaSUN, L.O.S., and Morph-Im platforms of the University of Namur. J. Mignon thanks the Belgian National Fund for Scientific Research (FNRS) for his FRIA PhD Student position. C. Michaux and D. Mottet also thank the FNRS for their Research Associate position. E. A. Perpète also thanks the FNRS for his Senior Research Associate position. This research did not receive any specific grant from funding agencies in the public, commercial, or not-for-profit sectors.
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