Journal of Biological Chemistry
Volume 285, Issue 44, 29 October 2010, Pages 33992-34003
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Signal Transduction
Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12*,

https://doi.org/10.1074/jbc.M110.134510Get rights and content
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Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 1:1 complex with Lys48-linked diUb, which it binds selectively over monoUb and Lys63-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys48-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.

Biophysics
NMR
Proteasome
Signal Transduction
Ubiquitin
X-ray Crystallography

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The atomic coordinates and structure factors (code 2X5N) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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*

This work was supported by the United Kingdom Medical Research Council, the Canadian Institutes of Health Research, and the Wellcome Trust.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Experimental Procedures and additional references, Figs. S1–S6, and Table S1.

1

These authors contributed equally to this work.