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Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC

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  • Yajuan Mu

    (Beijing University of Chemical Technology)

  • Yue Wang

    (Beijing University of Chemical Technology)

  • Yanfei Huang

    (Beijing University of Chemical Technology)

  • Dong Li

    (Beijing University of Chemical Technology)

  • Youyou Han

    (Beijing University of Chemical Technology)

  • Min Chang

    (Beijing University of Chemical Technology)

  • Jiaqi Fu

    (Purdue University)

  • Yongchao Xie

    (Beijing University of Chemical Technology)

  • Jie Ren

    (Chinese Academy of Agricultural Sciences)

  • Hao Wang

    (Beijing University of Chemical Technology)

  • Yi Zhang

    (Beijing University of Chemical Technology)

  • Zhao-Qing Luo

    (Purdue University)

  • Yue Feng

    (Beijing University of Chemical Technology)

Abstract

Protein ubiquitination is one of the most prevalent post-translational modifications, controlling virtually every process in eukaryotic cells. Recently, the Legionella effector MavC was found to mediate a unique ubiquitination through transglutamination, linking ubiquitin (Ub) to UBE2N through UbGln40 in a process that can be inhibited by another Legionella effector, Lpg2149. Here, we report the structures of MavC/UBE2N/Ub ternary complex, MavC/UBE2N-Ub (product) binary complex, and MavC/Lpg2149 binary complex. During the ubiquitination, the loop containing the modification site K92 of UBE2N undergoes marked conformational change, and Lpg2149 inhibits this ubiquitination through competing with Ub to bind MavC. Moreover, we found that MavC itself also exhibits weak deubiquitinase activity towards this non-canonical ubiquitination. Together, our study not only provides insights into the mechanism and inhibition of this transglutaminase-induced ubiquitination by MavC, but also sheds light on the future studies into UBE2N inhibition by this modification and deubiquitinases of this unique ubiquitination.

Suggested Citation

  • Yajuan Mu & Yue Wang & Yanfei Huang & Dong Li & Youyou Han & Min Chang & Jiaqi Fu & Yongchao Xie & Jie Ren & Hao Wang & Yi Zhang & Zhao-Qing Luo & Yue Feng, 2020. "Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15645-7
    DOI: 10.1038/s41467-020-15645-7
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