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

关键词：

D O I：

暂无

中图分类号：

学科分类号：

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.

引用

页码：120 / 124

页数：4

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