Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

被引:0
作者
Jiazhang Qiu
Michael J. Sheedlo
Kaiwen Yu
Yunhao Tan
Ernesto S. Nakayasu
Chittaranjan Das
Xiaoyun Liu
Zhao-Qing Luo
机构
[1] Purdue Institute for Inflammation,Immunology and Infectious Disease and Department of Biological Sciences
[2] Purdue University,Department of Chemistry
[3] Purdue University,Biological Science Division
[4] Institute of Analytical Chemistry and Synthetic and Functional Biomolecules Center,undefined
[5] College of Chemistry and Molecular Engineering,undefined
[6] Peking University,undefined
[7] Pacific Northwest National Laboratory,undefined
[8] Present address: Division of Gastroenterology,undefined
[9] Boston Children’s Hospital,undefined
[10] Harvard Medical School,undefined
[11] Boston,undefined
[12] Massachusetts 02115,undefined
[13] USA.,undefined
来源
Nature | 2016年 / 533卷
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摘要
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.
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页码:120 / 124
页数:4
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