A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge
- CNRS UMR 8576, University of Lille1, 59655 Villeneuve d’Ascq (France)
- Plate-forme BICeL-IFR142, Institut Pasteur de Lille, Lille (France)
- Inserm U1003, Laboratoire de physiologie cellulaire, Université Lille 1, 59650 Villeneuve d’Ascq (France)
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.
- OSTI ID:
- 22416301
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 445, 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); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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