Thapaliya, Arjun, Nyathi, Yvonne, Martínez-Lumbreras, Santiago , Krysztofinska, Ewelina M., Evans, Nicola J., Terry, Isabelle L., High, Stephen and Isaacson, Rivka L. (2016) SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism. Scientific Reports, 6 (1). p. 36622. ISSN 2045-2322
Full content URL: http://dx.doi.org/10.1038/srep36622
Documents |
|
|
PDF
srep36622.pdf - Whole Document Available under License Creative Commons Attribution 4.0 International. 2MB |
Item Type: | Article |
---|---|
Item Status: | Live Archive |
Abstract
The fate of secretory and membrane proteins that mislocalize to the cytosol is decided by a collaboration between cochaperone SGTA (small, glutamine-rich, tetratricopeptide repeat protein alpha) and the BAG6 complex, whose operation relies on multiple transient and subtly discriminated interactions with diverse binding partners. These include chaperones, membrane-targeting proteins and ubiquitination enzymes. Recently a direct interaction was discovered between SGTA and the proteasome, mediated by the intrinsic proteasomal ubiquitin receptor Rpn13. Here, we structurally and biophysically characterize this binding and identify a region of the Rpn13 C-terminal domain that is necessary and sufficient to facilitate it. We show that the contact occurs through a carboxylate clamp-mediated molecular recognition event with the TPR domain of SGTA, and provide evidence that the interaction can mediate the association of Rpn13 and SGTA in a cellular context.
Keywords: | Solution state NMR, Molecular conformation, Structural biology, JCOpen |
---|---|
Subjects: | C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry |
Divisions: | College of Science > School of Life Sciences |
ID Code: | 27023 |
Deposited On: | 20 Jun 2017 13:15 |
Repository Staff Only: item control page