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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
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    References listed on IDEAS

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    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.
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    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

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