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

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 and Yue Feng ()
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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

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-15645-7

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