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Ubiquitination independent of E1 and E2 enzymes by bacterial effectors

Author

Listed:
  • 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
    Present address: Division of Gastroenterology, Boston Children’s Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.)

  • 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)

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.

Suggested Citation

  • Jiazhang Qiu & Michael J. Sheedlo & Kaiwen Yu & Yunhao Tan & Ernesto S. Nakayasu & Chittaranjan Das & Xiaoyun Liu & Zhao-Qing Luo, 2016. "Ubiquitination independent of E1 and E2 enzymes by bacterial effectors," Nature, Nature, vol. 533(7601), pages 120-124, May.
    • Handle: RePEc:nat:nature:v:533:y:2016:i:7601:d:10.1038_nature17657
    DOI: 10.1038/nature17657
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    Citations

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    Cited by:

    1. Zhengrui Zhang & Jiaqi Fu & Johannes Gregor Matthias Rack & Chuang Li & Jim Voorneveld & Dmitri V. Filippov & Ivan Ahel & Zhao-Qing Luo & Chittaranjan Das, 2024. "Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Xiangkai Zhen & Yongyu Wu & Jinli Ge & Jiaqi Fu & Le Ye & Niannian Lin & Zhijie Huang & Zihe Liu & Zhao-qing Luo & Jiazhang Qiu & Songying Ouyang, 2022. "Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Michael Adams & Rahul Sharma & Thomas Colby & Felix Weis & Ivan Matic & Sagar Bhogaraju, 2021. "Structural basis for protein glutamylation by the Legionella pseudokinase SidJ," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    4. Yuen-Yan Chang & Camila Valenzuela & Arthur Lensen & Noelia Lopez-Montero & Saima Sidik & John Salogiannis & Jost Enninga & John Rohde, 2024. "Microtubules provide force to promote membrane uncoating in vacuolar escape for a cyto-invasive bacterial pathogen," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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