Abstract
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 Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-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.
Original language | English |
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Pages (from-to) | 33992-4003 |
Number of pages | 12 |
Journal | Journal of Biological Chemistry |
Volume | 285 |
Issue number | 44 |
DOIs | |
Publication status | Published - 29 Oct 2010 |
Keywords / Materials (for Non-textual outputs)
- Calorimetry
- Carrier Proteins
- Humans
- Kinetics
- Lysine
- Magnetic Resonance Spectroscopy
- Polyubiquitin
- Proteasome Endopeptidase Complex
- Protein Binding
- Schizosaccharomyces
- Schizosaccharomyces pombe Proteins
- Signal Transduction
- Surface Plasmon Resonance
- Ubiquitin
- von Willebrand Factor