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Self-stabilization mechanism encoded by a bacterial toxin facilitates reproductive parasitism

2023; Elsevier BV; Volume: 33; Issue: 18 Linguagem: Inglês

10.1016/j.cub.2023.08.032

1879-0445

Toshiyuki Harumoto,

Trypanosoma species research and implications

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Aldrich J.C. Akbari O.S. Ferree P.M. Male-killing Spiroplasma alters behavior of the dosage compensation complex during Drosophila melanogaster embryogenesis. Curr. Biol. 2016; 26: 1339-1345https://doi.org/10.1016/j.cub.2016.03.050 Abstract Full Text Full Text PDF PubMed Scopus (21) Google Scholar ,23 Harumoto T. Anbutsu H. Lemaitre B. Fukatsu T. Male-killing symbiont damages host's dosage-compensated sex chromosome to induce embryonic apoptosis. Nat. Commun. 2016; 712781https://doi.org/10.1038/ncomms12781 Crossref PubMed Scopus (36) Google Scholar Here, I show that without the function of OTU, Spaid is polyubiquitinated and degraded through the host ubiquitin-proteasome pathway, leading to the attenuation of male-killing activity as shown previously. 6 Harumoto T. Lemaitre B. Male-killing toxin in a bacterial symbiont of Drosophila. Nature. 2018; 557: 252-255https://doi.org/10.1038/s41586-018-0086-2 Crossref PubMed Scopus (83) Google Scholar Furthermore, I find that Spaid utilizes its OTU domain to deubiquitinate itself in an intermolecular manner. Collectively, the deubiquitinase domain of Spaid serves as a self-stabilization mechanism to facilitate male killing in flies, optimizing a molecular strategy of endosymbionts that enables the efficient manipulation of the host at a low energetic cost.