Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner

Genes Cells. 2011 May;16(5):545-56. doi: 10.1111/j.1365-2443.2011.01510.x. Epub 2011 Apr 1.

Abstract

We report a new type of interaction between two yeast prion proteins, Sup35 and New1. New1 consists of an N-terminal prion region (New1N) and a C-terminal region homologous to a translation elongation factor with two ATP-binding motifs. Amyloid formation of the Sup35 prion region (Sup35NM) was accelerated by a small amount of sonicated New1N amyloid (New1N-seeds) to produce Sup35NM[New1] amyloid. New1N amyloid formation was accelerated by Sup35NM[New1]-seeds but not by spontaneously generated Sup35NM-seeds, indicating that the structural features of the New1N amyloid were transmitted via the Sup35NM amyloid. Surprisingly, full-length New1 broke the Sup35NM amyloid fibrils in an ATP-dependent manner. This activity of New1 was independent from Hsp104. It was lost by a mutation in the second ATP-binding motif, by the truncation of the N-terminal prion region of New1 and by the pre-incubation of New1 with New1N-seeds. When New1 was overproduced in yeast [PSI(+)] cells carrying GFP-fused Sup35NM, diverse morphological changes in fluorescent foci occurred. Thus, New1 potentially has a regulatory role in prion state in yeast, working independently of the Hsp104 system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Amino Acid Sequence
  • Amyloid / genetics
  • Amyloid / metabolism*
  • Asparagine / genetics
  • Asparagine / metabolism
  • Binding Sites / genetics
  • Blotting, Western
  • Glutamine / genetics
  • Glutamine / metabolism
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Mutation
  • Peptide Termination Factors / genetics
  • Peptide Termination Factors / metabolism*
  • Prions / genetics
  • Prions / metabolism*
  • Protein Binding
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Amyloid
  • Heat-Shock Proteins
  • New1 protein, S cerevisiae
  • Peptide Termination Factors
  • Prions
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Glutamine
  • HsP104 protein, S cerevisiae
  • Green Fluorescent Proteins
  • Asparagine
  • Adenosine Triphosphate