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

Isabelle Huvent (1, 2) , Amina Kamah (1, 2) , François-Xavier Cantrelle (1, 2) , Nicolas Barois (3) , Christian Slomianny (4) , Caroline Smet-Nocca (1, 2) , Isabelle Landrieu (2, 1) , Guy Lippens (2, 1)

1 Université Lille Nord de France (COMUE)
2 UGSF - Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576
3 BICeL - Plateforme BioImaging Center Lille - PLBS
4 PHYCELL - Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U 1003

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.

Mots clés: Aggregation; Electron microscopy; NMR spectroscopy; Nucleation; Tau

Domaines: Biochimie [q-bio.BM]

Isabelle Huvent, Amina Kamah, François-Xavier Cantrelle, Nicolas Barois, Christian Slomianny, et al.. A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge.. Biochemical and Biophysical Research Communications, 2014, 445 (2), pp.299-303. ⟨10.1016/j.bbrc.2014.01.161⟩. ⟨hal-01077911⟩