1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p.
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.
Chen
Tony
T
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.
Zhang
Daoning
D
Matiuhin
Yulia
Y
Glickman
Michael
M
Fushman
David
D
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D018797:Cell Cycle Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry*; D014452:Ubiquitins / Q000737:chemistry*
D002247:Carbon Isotopes; D018797:Cell Cycle Proteins; C100415:DSK2 protein, S cerevisiae; D009587:Nitrogen Isotopes; D011522:Protons; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D014452:Ubiquitins