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1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p.

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 (1)H, (15)N, and (13)C 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.

SUBMITTER: Chen T

PROVIDER: S-EPMC2892233 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p.

Chen Tony T Zhang Daoning D Matiuhin Yulia Y Glickman Michael M Fushman David D

Biomolecular NMR assignments 20080829 2

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 (1)H, (15)N, and (13)C 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 ...[more]

PMID: 19636891

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