期刊
FASEB JOURNAL
卷 34, 期 10, 页码 13711-13725出版社
WILEY
DOI: 10.1096/fj.202000759RR
关键词
cell division; degradation of ubiquitinylated proteins; retroviral aspartic protease activity; Toxoplasma gondii; UBL-UBA shuttle protein family
资金
- National Natural Science Foundation of China [81971964, 31730096, 31672544]
Toxoplasma gondiiis an obligate intracellular apicomplexan parasite that causes lethal diseases in immunocompromised patients. Ubiquitin-proteasome system (UPS) regulates many cellular processes by degrading ubiquitinylated proteins. The UBL-UBA shuttle protein family, which escorts the ubiquitinylated proteins to the proteasome for degradation, are crucial components of UPS. Here, we identified three UBL-UBA shuttle proteins (TGGT1_304680, DNA damage inducible protein 1, DDI1; TGGT1_295340, UV excision repair protein rad23 protein, RAD23; and TGGT1_223680, ubiquitin family protein, DSK2) localized in the cytoplasm and nucleus ofT gondii. Deletion of shuttle proteins inhibited parasites growth and resulted in accumulation of ubiquitinylated proteins. Cell division of triple-gene knockout strain was asynchronous. In addition, we found that the retroviral aspartic protease activity of the nonclassical shuttle protein DDI1 was important for the virulence ofToxoplasmain mice. These results showed the critical roles of UBL-UBA shuttle proteins in regulating the degradation of ubiquitinylated proteins and cell division ofT gondii.
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