Peptide and protein binding in the axial channel of hsp104

HIGHLIGHTS

• who: Ronnie Lum from the Ronnie Lum1, Monika Niggemann, and John RGlover, From the Department of Biochemistry, University of Toronto, Ontario M S , Canada The AAAⴙ molecular chaperone Hsp, mediates the extraction of proteins from aggregates by unfolding and threading them through its axial channel in an ATP-driven process. An Hsp104-binding peptide selected from solid phase arrays enhanced the refolding of a firefly luciferase-peptide fusion protein. Analysis of peptide binding using tryptophan fluorescence revealed two distinct binding sites, one in each AAAⴙ module of Hsp104. As a further indication of the relevance of peptide . . .
  

   

  

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