Journal article

Molecular and structural insight into lysine selection on substrate and ubiquitin lysine 48 by the ubiquitin-conjugating enzyme Cdc34

Randy Suryadinata, Jessica K Holien, George Yang, Michael W Parker, Elena Papaleo, Boris Sarcevic



The attachment of ubiquitin (Ub) to lysines on substrates or itself by ubiquitin-conjugating (E2) and ubiquitin ligase (E3) enzymes results in protein ubiquitination. Lysine selection is important for generating diverse substrate-Ub structures and targeting proteins to different fates; however, the mechanisms of lysine selection are not clearly understood. The positioning of lysine(s) toward the E2/E3 active site and residues proximal to lysines are critical in their selection. We investigated determinants of lysine specificity of the ubiquitin-conjugating enzyme Cdc34, toward substrate and Ub lysines. Evaluation of the relative importance of different residues positioned -2, -1, +1 and +2 t..

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Awarded by National Health and Medical Research Council

Funding Acknowledgements

We thank Prof. Mike Tyers, Samuel Lunenfeld Research Institute, Mount Sinai Hospital (Toronto, Ontario Canada) for Cdc4 baculovirus. This research was supported by grant 620205 from the National Health and Medical Research Council to B. S. and a National Health and Medical Research Council Research Fellowship to M. W. P. We acknowledge the support of the Victorian State Government Operational Infrastructure Support Program to St. Vincent's Institute.