IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v533y2016i7601d10.1038_nature17657.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature17657
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature17657?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    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. Kristin M. Kotewicz & Mengyun Zhang & Seongok Kim & Meghan S. Martin & Atish Roy Chowdhury & Albert Tai & Rebecca A. Scheck & Ralph R. Isberg, 2024. "Sde proteins coordinate ubiquitin utilization and phosphoribosylation to establish and maintain the Legionella replication vacuole," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. 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.
    4. Jiaqi Fu & Siying Li & Hongxin Guan & Chuang Li & Yan-Bo Zhao & Tao-Tao Chen & Wei Xian & Zhengrui Zhang & Yao Liu & Qingtian Guan & Jingting Wang & Qiuhua Lu & Lina Kang & Si-Ru Zheng & Jinyu Li & Sh, 2024. "Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    5. 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.
    6. Min Wan & Marena E. Minelli & Qiuye Zhao & Shannon Marshall & Haiyuan Yu & Marcus Smolka & Yuxin Mao, 2024. "Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognition," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    7. 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.
    8. Minhyeong Choi & Minwoo Jeong & Sangwoo Kang & Hayoung Jeon & Donghyuk Shin, 2024. "Legionella pneumophila evades host-autophagic clearance using phosphoribosyl-polyubiquitin chains," Nature Communications, Nature, vol. 15(1), pages 1-4, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:533:y:2016:i:7601:d:10.1038_nature17657. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.