skip to main content

Title: A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge

Highlights: • A functional fragment of Tau forms bundled ribbon-like fibrils. • Nucleation of its fibril formation is faster than for full-length Tau. • In contrast to full-length Tau, without cysteines, the fragment still forms fibers. - Abstract: We study the aggregation of a fragment of the neuronal protein Tau that contains part of the proline rich domain and of the microtubule binding repeats. When incubated at 37 °C with heparin, the fragment readily forms fibers as witnessed by Thioflavin T fluorescence. Electron microscopy and NMR spectroscopy show bundled ribbon like structures with most residues rigidly incorporated in the fibril. Without its cysteines, this fragment still forms fibers of a similar morphology, but with lesser Thioflavin T binding sites and more mobility for the C-terminal residues.
Authors:
; ;  [1] ;  [2] ;  [3] ; ;  [1] ;  [1]
  1. CNRS UMR 8576, University of Lille1, 59655 Villeneuve d’Ascq (France)
  2. Plate-forme BICeL-IFR142, Institut Pasteur de Lille, Lille (France)
  3. Inserm U1003, Laboratoire de physiologie cellulaire, Université Lille 1, 59650 Villeneuve d’Ascq (France)
Publication Date:
OSTI Identifier:
22416301
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 445; Journal Issue: 2; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ABSORPTION SPECTROSCOPY; AGGLOMERATION; CYSTEINE; ELECTRON MICROSCOPY; FIBERS; FLUORESCENCE; HEPARIN; MICROTUBULES; MOBILITY; MORPHOLOGY; NMR SPECTRA; NUCLEAR MAGNETIC RESONANCE; NUCLEATION; PROLINE; PROTEINS; RESIDUES