Nakasone, M. and Huang, D. T. (2016) Ubiquitination accomplished: E1 and E2 enzymes were not necessary. Molecular Cell, 62(6), pp. 807-809. (doi: 10.1016/j.molcel.2016.06.001) (PMID:27315555)
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120922.pdf - Accepted Version 664kB |
Abstract
Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.
| Item Type: | Articles (Other) |
|---|---|
| Additional Information: | This work was funded by Cancer Research UK and ERC grant number 647849. |
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Huang, Professor Danny |
| Authors: | Nakasone, M., and Huang, D. T. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
| Journal Name: | Molecular Cell |
| Publisher: | Cell Press |
| ISSN: | 1097-2765 |
| ISSN (Online): | 1097-4164 |
| Published Online: | 16 June 2016 |
| Copyright Holders: | Copyright © 2016 Cell Press |
| First Published: | First published in Molecular Cell 62(6):807-809 |
| Publisher Policy: | Reproduced in accordance with the copyright policy of the publisher |
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