Structural elucidation of recombinant <i>Trichomonas vaginalis</i> 20S proteasome bound to covalent inhibitors.

ABSTRACT: Proteasomes are essential for protein homeostasis in mammalian cells^1-4 and in protozoan parasites such as Trichomonas vaginalis (Tv).⁵ Tv and other protozoan 20S proteasomes have been validated as druggable targets.^6-8 However, in the case of Tv 20S proteasome (Tv20S), biochemical and structural studies were impeded by low yields and purity of the native proteasome. We successfully made recombinant Tv20S by expressing all seven α and seven β subunits together with the Ump-1 chaperone in insect cells. We isolated recombinant proteasome and showed that it was biochemically indistinguishable from the native enzyme. We confirmed that the recombinant Tv20S is inhibited by the natural product marizomib (MZB)⁹

SUBMITTER: Silhan J 

PROVIDER: S-EPMC10462138 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature