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

Biochem Biophys Res Commun. 2014 Mar 7;445(2):299-303. doi: 10.1016/j.bbrc.2014.01.161. Epub 2014 Feb 3.

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.

Keywords: Aggregation; Electron microscopy; NMR spectroscopy; Nucleation; Tau.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cysteine / chemistry*
  • Cysteine / metabolism
  • Heparin / metabolism
  • Humans
  • Magnetic Resonance Spectroscopy
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / ultrastructure
  • tau Proteins / chemistry*
  • tau Proteins / metabolism
  • tau Proteins / ultrastructure*

Substances

  • Recombinant Proteins
  • tau Proteins
  • Heparin
  • Cysteine