These authors contributed equally.
A Pyrrolysine Analogue for Site-Specific Protein Ubiquitination†
Article first published online: 30 OCT 2009
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 48, Issue 48, pages 9184–9187, November 16, 2009
How to Cite
Li, X., Fekner, T., Ottesen, Jennifer J. and Chan, Michael K. (2009), A Pyrrolysine Analogue for Site-Specific Protein Ubiquitination. Angew. Chem. Int. Ed., 48: 9184–9187. doi: 10.1002/anie.200904472
This research was supported by a grant from the US National Institutes of Health (GM061796) and an American Heart Association Great Rivers Affiliate Predoctoral Fellowship (0815449D) to X.L. We also thank the staff of the CCIC Mass Spectrometry and Proteomics Facility at OSU for protein analysis by mass spectrometry, Professor Michael Zhu (OSU) for providing Rattus norvegicus CaM cDNA, and Professor Bing Hao (UConn) for the human ubiquitin cDNA.
- Issue published online: 11 NOV 2009
- Article first published online: 30 OCT 2009
- Manuscript Received: 10 AUG 2009
- US National Institutes of Health. Grant Number: GM061796
- native chemical ligation;
- protein engineering;
- protein modifications;
The art of stitching proteins: D-Cys-ε-Lys and its diastereomer L-Cys-ε-Lys read through the UAG codon (see scheme). As the resulting proteins can participate in native chemical ligation (NCL), this process provides a means to prepare proteins chemoselectively modified (e.g. ubiquitinated) through a peptidic side chain located at the ε position of a rationally selected lysine residue.