+検索条件
-Structure paper
タイトル | CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. |
---|---|
ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 107, Issue 18, Page 8135-8140, Year 2010 |
掲載日 | 2010年5月4日 |
著者 | Sukyeong Lee / Bernhard Sielaff / Jungsoon Lee / Francis T F Tsai / |
PubMed 要旨 | 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:20404203 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 11.0 - 11.1 Å |
構造データ | EMDB-1629: EMDB-1630: EMDB-1631: |
由来 |
|