Molecular Basis for Lysine Specificity in the Yeast Ubiquitin-Conjugating Enzyme Cdc34
Martin Sadowski, Randy Suryadinata, Xianning Lai, Joerg Heierhorst, Boris Sarcevic
MOLECULAR AND CELLULAR BIOLOGY | AMER SOC MICROBIOLOGY | Published : 2010
Ubiquitin (Ub)-conjugating enzymes (E2s) and ubiquitin ligases (E3s) catalyze the attachment of Ub to lysine residues in substrates and Ub during monoubiquitination and polyubiquitination. Lysine selection is important for the generation of diverse substrate-Ub structures, which provides versatility to this pathway in the targeting of proteins to different fates. The mechanisms of lysine selection remain poorly understood, with previous studies suggesting that the ubiquitination site(s) is selected by the E2/E3-mediated positioning of a lysine(s) toward the E2/E3 active site. By studying the polyubiquitination of Sic1 by the E2 protein Cdc34 and the RING E3 Skp1/Cul1/F-box (SCF) protein, we ..View full abstract
This research was supported by grants from the Cancer Council Victoria, the Multiple Myeloma Research Foundation, and the Association for International Cancer Research.