IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-32364-3.html
   My bibliography  Save this article

Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains

Author

Listed:
  • Lining Lu

    (Guangxi University
    Tsinghua University)

  • Xiaoguo Zhai

    (Guangxi University)

  • Xiaolong Li

    (Beijing Institute of Technology)

  • Shuansuo Wang

    (Shanxi Agricultural University
    Chinese Academy of Sciences)

  • Lijun Zhang

    (Guangxi University)

  • Luyang Wang

    (Guangxi University)

  • Xi Jin

    (Guangxi University)

  • Lujun Liang

    (Tsinghua University)

  • Zhiheng Deng

    (Tsinghua University)

  • Zichen Li

    (Tsinghua University)

  • Yanfeng Wang

    (Beijing Institute of Technology)

  • Xiangdong Fu

    (Chinese Academy of Sciences)

  • Honggang Hu

    (Tsinghua University
    Shanghai University)

  • Jiawei Wang

    (Tsinghua University)

  • Ziqing Mei

    (University of Science and Technology Beijing)

  • Zhengguo He

    (Guangxi University)

  • Feng Wang

    (Beijing Institute of Technology)

Abstract

Linear (Met1-linked) ubiquitination is involved inflammatory and innate immune signaling. Previous studies have characterized enzymes regulating the addition and removal of this modification in mammalian systems. However, only a few plant-derived deubiquitinases targeting Met1-linked ubiquitin chains have been reported and their mechanism of action remains elusive. Here, using a dehydroalanine-bearing Met1-diubiquitin suicide probe, we discover OTUB1 from Oryza sativa (OsOTUB1) as a Met1-linked ubiquitin chain-targeting deubiquitinase. By solving crystal structures of apo OsOTUB1 and an OsOTUB1/Met1-diubiquitin complex, we find that Met1 activity is conferred by Met1-specific motifs in the S1’ pocket of OsOTUB1. Large-scale sequence alignments and hydrolysis experiments provide evidence that these motifs are a general determinant of Met1 activity in the OTUB subfamily across species. Analysis of the species distribution of OTUBs capable of hydrolysing Met1-linked ubiquitin chains shows that this activity is conserved in green plants (Viridiplantae) and does not exist in metazoans, providing insights into the evolutionary differentiation between primitive plants and animals.

Suggested Citation

  • Lining Lu & Xiaoguo Zhai & Xiaolong Li & Shuansuo Wang & Lijun Zhang & Luyang Wang & Xi Jin & Lujun Liang & Zhiheng Deng & Zichen Li & Yanfeng Wang & Xiangdong Fu & Honggang Hu & Jiawei Wang & Ziqing , 2022. "Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32364-3
    DOI: 10.1038/s41467-022-32364-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-32364-3
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-32364-3?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
    ---><---

    References listed on IDEAS

    as
    1. Fumiyo Ikeda & Yonathan Lissanu Deribe & Sigrid S. Skånland & Benjamin Stieglitz & Caroline Grabbe & Mirita Franz-Wachtel & Sjoerd J. L. van Wijk & Panchali Goswami & Vanja Nagy & Janos Terzic & Fumin, 2011. "SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis," Nature, Nature, vol. 471(7340), pages 637-641, March.
    Full references (including those not matched with items on IDEAS)

    Citations

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


    Cited by:

    1. Hossam S. El-Beltagi & Khairiah Mubarak Alwutayd & Umair Rasheed & Abdul Sattar & Qasim Ali & Basmah M. Alharbi & Ghadah Hamad Al-Hawas & Zahid Khorshid Abbas & Doaa Bahaa Eldin Darwish & Samy F. Mahm, 2024. "Sole and combined foliar application of silicon and putrescine alleviates the negative effects of drought stress in maize by modulating the morpho-physiological and antioxidant defence mechanisms," Plant, Soil and Environment, Czech Academy of Agricultural Sciences, vol. 70(1), pages 26-39.
    2. repec:caa:jnlpse:v:preprint:id:423-2023-pse is not listed on IDEAS

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yi Luan & Wenying Long & Lisi Dai & Panfeng Tao & Zhifen Deng & Zongping Xia, 2024. "Linear ubiquitination regulates the KSHV replication and transcription activator protein to control infection," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Esther Hoste & Kim Lecomte & Karl Annusver & Niels Vandamme & Jana Roels & Sophia Maschalidi & Lien Verboom & Hanna-Kaisa Vikkula & Mozes Sze & Lisette Van Hove & Kevin Verstaen & Arne Martens & Tino , 2021. "OTULIN maintains skin homeostasis by controlling keratinocyte death and stem cell identity," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    3. Xiangyi S. Wang & Thomas R. Cotton & Sarah J. Trevelyan & Lachlan W. Richardson & Wei Ting Lee & John Silke & Bernhard C. Lechtenberg, 2023. "The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    4. Hannah Schünke & Ulrike Göbel & Ivan Dikic & Manolis Pasparakis, 2021. "OTULIN inhibits RIPK1-mediated keratinocyte necroptosis to prevent skin inflammation in mice," Nature Communications, Nature, vol. 12(1), pages 1-15, 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:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32364-3. 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.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with 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.