Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

Jiazhang Qiu, Michael J. Sheedlo, Kaiwen Yu, Yunhao Tan, Ernesto S. Nakayasu, Chittaranjan Das, Xiaoyun Liu and Zhao-Qing Luo ()
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Jiazhang Qiu: Purdue Institute for Inflammation, Purdue University
Michael J. Sheedlo: Purdue University
Kaiwen Yu: Institute of Analytical Chemistry and Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University
Yunhao Tan: Purdue Institute for Inflammation, Purdue University
Ernesto S. Nakayasu: Pacific Northwest National Laboratory
Chittaranjan Das: Purdue University
Xiaoyun Liu: Institute of Analytical Chemistry and Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University
Zhao-Qing Luo: Purdue Institute for Inflammation, Purdue University

Nature, 2016, vol. 533, issue 7601, 120-124

Abstract: An unprecedented mechanism of ubiquitination that is independent of E1 and E2 enzymes, instead relying on activation of ubiquitin by ADP-ribosylation, and which is mediated by members of the SidE effector family encoded by the bacterial pathogen Legionella pneumophila, establishes that ubiquitination can be carried out by a single enzyme.

Date: 2016
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DOI: 10.1038/nature17657

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