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Logo of nihpaAbout Author manuscriptsSubmit a manuscriptHHS Public Access; Author Manuscript; Accepted for publication in peer reviewed journal;
 
From:
Biochim Biophys Acta. Author manuscript; available in PMC 2013 January 1.
Published in final edited form as:
Biochim Biophys Acta. 2012 January; 1823(1): 29–39.
Published online 2011 July 24. doi: 10.1016/j.bbamcr.2011.07.014

Figure 1

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In vitro disaggregase activity of Hsp104 and ClpB

(a) Hsp104 remodels amorphous aggregates via collaboration with Hsp70 and Hsp40, while ClpB remodels these types of aggregates via collaboration with DnaK, DnaJ, and GrpE (KJE). The product of disaggregation of amorphous aggregates is natively folded protein. Hsp104 or ClpB hexamer is shown in gray with the front half cutaway to reveal the axial channel running down the length of the structure. Four pore loops with conserved tyrosines residues are shown in orange. These pore loops are important for substrate binding and threading through the axial channel. (b) Only Hsp104 is able to remodel amyloid aggregates and in vitro this can proceed without the aid of Hsp70 and Hsp40. Products of amyloid disaggregation are soluble natively folded protein and fragmented amyloids. However, for some amyloids (e.g. Sup35 prions) remodeling can continue to generate disordered-type aggregates that Hsp104 cannot remodel and which lack the seeding activity of amyloid [23].

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