1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p |
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| Authors: | Tony Chen Daoning Zhang Yulia Matiuhin Michael Glickman David Fushman |
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| Institution: | (1) Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, 1115 Biomolecular Sciences Building (#296), College Park, MD 20742-3360, USA;(2) Department of Biology, The Technion—Israel Institute of Technology, Haifa, Israel |
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| Abstract: | The ubiquitin-like domain (UBL) of yeast protein Dsk2p is widely believed to recognize and bind to ubiquitin receptors on
the proteasome and, as part of Dsk2p, to bridge polyubiquitinated substrates and proteasomal degradation machinery. Here we
report NMR resonance assignment for 1H, 15N, and 13C nuclei in the backbone and side chains of the UBL domain of Dsk2p. This assignment will aid in NMR studies focused on understanding
of Dsk2’s interactions with proteasomal receptors and its role as a polyubiquitin shuttle in the ubiquitin-dependent proteasomal
degradation as well as other cellular pathways. |
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| Keywords: | Dsk2p Ubiquitin-like domain UBL Proteasome |
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