Molecular and structural architecture of polyQ aggregates in yeast

  • Anselm Gruber
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Daniel Hornburg
    Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Matthias Antonin
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Natalie Krahmer
    Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Javier Collado
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Miroslava Schaffer
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Greta Zubaite
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Christian Lüchtenborg
    Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
  • Timo Sachsenheimer
    Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
  • Britta Brügger
    Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
  • Matthias Mann
    Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Wolfgang Baumeister
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • F. Ulrich Hartl
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Mark S. Hipp
    Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
  • Rubén Fernández-Busnadiego
    Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;

抄録

<jats:title>Significance</jats:title> <jats:p>How protein aggregation leads to neurodegenerative disorders such as Huntington’s disease remains poorly understood. Here we show that polyglutamine (polyQ) aggregation in yeast results in the formation of amorphous inclusions and less frequent fibrils. This is accompanied by significant changes in proteome composition as well as distortions in mitochondria and lipid droplet morphology that do not arise from direct interactions of these organelles with polyQ inclusions or fibrils. This contrasts with recent observations in mammalian cells, where the same polyQ proteins formed amyloid-like fibrils that distort endoplasmic reticulum membranes. These results demonstrate that the same polyQ expansion protein can adopt different nonnative conformations that utilize distinct mechanisms to target a variety of cellular structures.</jats:p>

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