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. 2020 Aug 21;10:448. doi: 10.3389/fcimb.2020.00448

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Copyright © 2020 Kitao, Nagai and Kubori.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Schemes of effector interplay in the regulation of unconventional ubiquitination and gene organization of sidEs, dupA/dupB, sidJ/sdjA, and mavC/mvcA loci in L. pneumophila. (A) SidEs are encoded in two loci in the L. pneumophila genome. sdeA, sdeB, and sdeC genes are in a cluster, and the sidE gene is in a separate locus. DupA is encoded in the same locus as sdeA, sdeB, and sdeC, while DupB is encoded in a different locus. SidJ is encoded in a locus with sdeA, sdeB, sdeC, and dupA. sdjA is thought to be a paralogue of sidJ, representing in the same locus with dupB. mavC and mvcA are tandem-arrayed paralogous genes adjacent to lpg2149. (B) SidEs have an equivalent function in PR-ubiquitination mediated by mART and PDE activities. Products of the paralogous genes dupA and dupB can reverse PR-ubiquitination with their unique deubiquitination activity. Together with the cofactor CaM, SidJ executes an enzymatic effect to glutamylate the active site of the mART domain of SidEs, thereby inhibiting SidEs-mediated ubiquitination (see text for details). (C) MavC and MvcA display deamidation activity against ubiquitin. MavC, but not MvcA, possesses a transglutamination activity and forms a covalent bond between ubiquitin and the E2 enzyme UBE2N. The unconventional ubiquitination of UBE2N can be reversed by the unique DUB activity of MvcA. Lpg2149 can prevent the deamidase activity of both MavC and MvcA. It can also prevent the DUB activity of MvcA (see text for details).