Willhoft, Oliver and Kerr, R. and Patel, Dipali and Zhang, Wenjuan and Al-Jassar, Caezar and Daviter, Tina and Millson, S. and Thalassinos, Konstantinos and Vaughan, Cara K. (2017) The crystal structure of the Sgt1-Skp1 complex: the link between Hsp90 and both SCF E3 ubiquitin ligases and kinetochores. Scientific Reports , p. 41626. ISSN 2045-2322.
![[img]](https://eprints.bbk.ac.uk/style/images/fileicons/text.png) |
Text
111550_1_merged_1479415281.pdf - Author's Accepted Manuscript Restricted to Repository staff only Download (9MB) |
|
|
Text
111550_1_supp_3449707_1gt01h_convrt.pdf - Supplemental Material Restricted to Repository staff only Download (5MB) |
|
|
Text
17956.pdf - Published Version of Record Available under License Creative Commons Attribution. Download (2MB) | Preview |
|
|
Text
17956A.pdf - Supplemental Material Available under License Creative Commons Attribution. Download (5MB) | Preview |
Abstract
The essential cochaperone Sgt1 recruits Hsp90 chaperone activity to a range of cellular factors including SCF E3 ubiquitin ligases and the kinetochore in eukaryotes. In these pathways Sgt1 interacts with Skp1, a small protein that heterodimerizes with proteins containing the F-box motif. We have determined the crystal structure of the interacting domains of Saccharomyces cerevisiae Sgt1 and Skp1 at 2.8 Å resolution and validated the interface in the context of the full-length proteins in solution. The BTB/POZ domain of Skp1 associates with Sgt1 via the concave surface of its TPR domain using residues that are conserved in humans. Dimerization of yeast Sgt1 occurs via an insertion that is absent from monomeric human Sgt1. We identify point mutations that disrupt dimerization and Skp1 binding in vitro and find that the interaction with Skp1 is an essential function of Sgt1 in yeast. Our data provide a structural rationale for understanding the phenotypes of temperature-sensitive Sgt1 mutants and for linking Skp1-associated proteins to Hsp90- dependent pathways.
Metadata
| Item Type: | Article |
|---|---|
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Cara Vaughan |
| Date Deposited: | 01 Feb 2017 16:11 |
| Last Modified: | 02 Aug 2023 17:30 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/17956 |
Statistics
Additional statistics are available via IRStats2.
Archive Staff Only (login required)
