Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins

Laura Masino, Geoff Kelly, Kevin Leonard, Yvon Trottier, Annalisa Pastore

Research output: Contribution to journalArticlepeer-review

140 Scopus citations

Abstract

Aggregation of expanded polyglutamine (polyQ) seems to be the cause of various genetic neurodegenerative diseases. Relatively little is known as yet about the polyQ structure and the mechanism that induces aggregation. We have characterised the solution structure of polyQ in a proteic context using a model system based on glutathione S-transferase fusion proteins. A wide range of biophysical techniques was applied. For the first time, nuclear magnetic resonance was used to observe directly and selectively the conformation of polyQ in the pathological range. We demonstrate that, in solution, polyQs are in a random coil conformation. However, under destabilising conditions, their aggregation behaviour is determined by the polyQ length.

Original languageEnglish
Pages (from-to)267-272
Number of pages6
JournalFEBS Letters
Volume513
Issue number2-3
DOIs
StatePublished - 27 Feb 2002
Externally publishedYes

Keywords

  • Aggregation
  • Glutathione S-transferase
  • Huntington
  • Polyglutamine
  • Structure

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