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-Structure paper
| Title | CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 107, Issue 18, Page 8135-8140, Year 2010 |
| Publish date | May 4, 2010 |
 Authors | Sukyeong Lee / Bernhard Sielaff / Jungsoon Lee / Francis T F Tsai /  |
| PubMed Abstract | Hsp104 is a ring-forming AAA+ machine that recognizes both aggregated proteins and prion-fibrils as substrates and, together with the Hsp70 system, remodels substrates in an ATP-dependent manner. ...Hsp104 is a ring-forming AAA+ machine that recognizes both aggregated proteins and prion-fibrils as substrates and, together with the Hsp70 system, remodels substrates in an ATP-dependent manner. Whereas the ability to disaggregate proteins is dependent on the Hsp104 M-domain, the location of the M-domain is controversial and its exact function remains unknown. Here we present cryoEM structures of two Hsp104 variants in both crosslinked and noncrosslinked form, in addition to the structure of a functional Hsp104 chimera harboring T4 lysozyme within the M-domain helix L2. Unexpectedly, we found that our Hsp104 chimera has gained function and can solubilize heat-aggregated beta-galactosidase (beta-gal) in the absence of the Hsp70 system. Our fitted structures confirm that the subunit arrangement of Hsp104 is similar to other AAA+ machines, and place the M-domains on the Hsp104 exterior, where they can potentially interact with large, aggregated proteins. |
 External links | Proc Natl Acad Sci U S A / PubMed:20404203 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 11.0 - 11.1 Å |
| Structure data |  EMDB-1629:  EMDB-1630:  EMDB-1631: |
| Source |
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Saccharomyces cerevisiae (brewer's yeast)